Catalase: Difference between revisions

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| TCDB =
| TCDB =
| CDD = cd00328
| CDD = cd00328
| OPM family = 435
| OPM family = 370
| OPM protein = 3e4w
| OPM protein = 3e4w
| PDB =
| PDB =
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}}
}}
{{Infobox_gene}}
{{Infobox_gene}}
'''Catalase''' is a common [[enzyme]] found in nearly all living organisms exposed to oxygen (such as [[bacteria]], plants, and animals). It [[catalyst|catalyzes]] the decomposition of [[hydrogen peroxide]] to [[water]] and [[oxygen]].<ref name="pmid14745498">{{cite journal | vauthors = Chelikani P, Fita I, Loewen PC | title = Diversity of structures and properties among catalases | journal = Cellular and Molecular Life Sciences | volume = 61 | issue = 2 | pages = 192–208 | date = January 2004 | pmid = 14745498 | doi = 10.1007/s00018-003-3206-5 | url = https://digital.csic.es/bitstream/10261/111097/1/accesoRestringido.pdf }}</ref> It is a very important enzyme in protecting the cell from [[oxidative stress|oxidative damage]] by [[reactive oxygen species]] (ROS). Likewise, catalase has one of the highest [[turnover number]]s of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.<ref>{{cite web | title = Catalase | author = Goodsell DS | work = Molecule of the Month | publisher = RCSB Protein Data Bank | url = http://pdb101.rcsb.org/motm/57 | date = 2004-09-01 | accessdate = 2016-08-23}}</ref>
'''Catalase''' is a common [[enzyme]] found in nearly all living organisms exposed to oxygen (such as [[bacteria]], plants, and animals). It [[catalyst|catalyzes]] the decomposition of [[hydrogen peroxide]] to [[water]] and [[oxygen]].<ref name="pmid14745498">{{cite journal | vauthors = Chelikani P, Fita I, Loewen PC | title = Diversity of structures and properties among catalases | journal = Cellular and Molecular Life Sciences | volume = 61 | issue = 2 | pages = 192–208 | date = January 2004 | pmid = 14745498 | doi = 10.1007/s00018-003-3206-5 | url = }}</ref> It is a very important enzyme in protecting the cell from [[oxidative stress|oxidative damage]] by [[reactive oxygen species]] (ROS). Likewise, catalase has one of the highest [[turnover number]]s of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.<ref>{{cite web | title = Catalase | author = Goodsell DS | work = Molecule of the Month | publisher = RCSB Protein Data Bank | url = http://pdb101.rcsb.org/motm/57 | date = 2004-09-01 | accessdate = 2016-08-23}}</ref>


Catalase is a [[Tetrameric protein|tetramer]] of four polypeptide chains, each over 500 [[amino acid]]s long.<ref name=Boon_a>{{cite web |vauthors=Boon EM, Downs A, Marcey D |title = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm | accessdate = 2007-02-11}}</ref> It contains four iron-containing [[heme]] groups that allow the enzyme to react with the hydrogen peroxide. The optimum [[pH]] for human catalase is approximately 7,<ref name="Maehly_1954">{{cite journal | vauthors = Maehly AC, Chance B | title = The assay of catalases and peroxidases | journal = Methods of Biochemical Analysis | volume = 1 | pages = 357–424 | year = 1954 | pmid = 13193536 | doi = 10.1002/9780470110171.ch14 | isbn = 978-0-470-11017-1 | series = Methods of Biochemical Analysis }}</ref> and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.<ref name="pmid6727660">{{cite journal | vauthors = Aebi H | title = Catalase in vitro | journal = Methods in Enzymology | volume = 105 | pages = 121–6 | year = 1984 | pmid = 6727660 | doi = 10.1016/S0076-6879(84)05016-3 | isbn = 978-0-12-182005-3 | series = Methods in Enzymology }}</ref> The pH optimum for other catalases varies between 4 and 11 depending on the species.<ref name="urlEC 1.11.1.6 - catalase">{{cite web | url = http://www.brenda-enzymes.org/php/result_flat.php4?ecno=1.11.1.6&Suchword=&organism%5B%5D=&show_tm=0 | title = EC 1.11.1.6 - catalase | format = | work = BRENDA: The Comprehensive Enzyme Information System | publisher = Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig | accessdate = 2009-05-26}}</ref> The optimum temperature also varies by species.<ref name=Bucknell>{{cite web | title = A Quantitative Enzyme Study; CATALASE |vauthors=Toner K, Sojka G, Ellis R | work = | publisher = bucknell.edu | url = http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html | accessdate = 2007-02-11 |archiveurl = https://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html |archivedate = 2000-06-12}}</ref>
Catalase is a [[Tetrameric protein|tetramer]] of four polypeptide chains, each over 500 [[amino acid]]s long.<ref name=Boon_a>{{cite web |vauthors=Boon EM, Downs A, Marcey D |title = Catalase: H<sub>2</sub>O<sub>2</sub>: H<sub>2</sub>O<sub>2</sub> Oxidoreductase | work = Catalase Structural Tutorial Text | url = http://biology.kenyon.edu/BMB/Chime/catalase/frames/cattx.htm | accessdate = 2007-02-11}}</ref> It contains four iron-containing [[heme]] groups that allow the enzyme to react with the hydrogen peroxide. The optimum [[pH]] for human catalase is approximately 7,<ref name="Maehly_1954">{{cite journal | vauthors = Maehly AC, Chance B | title = The assay of catalases and peroxidases | journal = Methods of Biochemical Analysis | volume = 1 | pages = 357–424 | year = 1954 | pmid = 13193536 | doi = 10.1002/9780470110171.ch14 | isbn = 978-0-470-11017-1 | series = Methods of Biochemical Analysis }}</ref> and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.<ref name="pmid6727660">{{cite journal | vauthors = Aebi H | title = Catalase in vitro | journal = Methods in Enzymology | volume = 105 | pages = 121–6 | year = 1984 | pmid = 6727660 | doi = 10.1016/S0076-6879(84)05016-3 | isbn = 978-0-12-182005-3 | series = Methods in Enzymology }}</ref> The pH optimum for other catalases varies between 4 and 11 depending on the species.<ref name="urlEC 1.11.1.6 - catalase">{{cite web | url = http://www.brenda-enzymes.org/php/result_flat.php4?ecno=1.11.1.6&Suchword=&organism%5B%5D=&show_tm=0 | title = EC 1.11.1.6 - catalase | format = | work = BRENDA: The Comprehensive Enzyme Information System | publisher = Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig | accessdate = 2009-05-26}}</ref> The optimum temperature also varies by species.<ref name=Bucknell>{{cite web | title = A Quantitative Enzyme Study; CATALASE |vauthors=Toner K, Sojka G, Ellis R | work = | publisher = bucknell.edu | url = http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html | accessdate = 2007-02-11 |archiveurl = https://web.archive.org/web/20000612104029/http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html |archivedate = 2000-06-12}}</ref>
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== Function ==
== Function ==


=== Action ===
=== Reaction ===
Catalase catalyzes the following reaction:
 
: 2 H<sub>2</sub>O<sub>2</sub> → 2 H<sub>2</sub>O + O<sub>2</sub>
: 2 H<sub>2</sub>O<sub>2</sub> → 2 H<sub>2</sub>O + O<sub>2</sub>


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The exact mechanism of this reaction is not known.
The exact mechanism of this reaction is not known.


Any heavy metal ion (such as copper cations in [[copper(II) sulfate]]) can act as a [[noncompetitive inhibitor]] of catalase. Furthermore, the poison [[cyanide]] is a [[competitive inhibitor]] of catalase at high concentrations of [[hydrogen peroxide]].<ref>{{cite journal | vauthors = Ogura Y, Yamazaki I | title = Steady-state kinetics of the catalase reaction in the presence of cyanide | journal = Journal of Biochemistry | volume = 94 | issue = 2 | pages = 403–8 | date = August 1983 | pmid = 6630165 | doi =  }}</ref>
Any heavy metal ion (such as copper cations in [[copper(II) sulfate]]) can act as a [[noncompetitive inhibitor]] of catalase. Furthermore, the poison [[cyanide]] is a noncompetitive inhibitor<ref>Nonstationary Inhibition of Enzyme Action. The Cyanide Inhibition of Catalase</ref> of catalase at high concentrations of [[hydrogen peroxide]].<ref>{{cite journal | vauthors = Ogura Y, Yamazaki I | title = Steady-state kinetics of the catalase reaction in the presence of cyanide | journal = Journal of Biochemistry | volume = 94 | issue = 2 | pages = 403–8 | date = August 1983 | pmid = 6630165 | doi =  10.1093/oxfordjournals.jbchem.a134369}}</ref>
[[Arsenate]] acts as an [[Enzyme activator|activator]].<ref>{{cite journal | vauthors = Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ | title = Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure | journal = Plant Physiology and Biochemistry | volume = 47 | issue = 10 | pages = 960–5 | date = October 2009 | pmid = 19574057 | doi = 10.1016/j.plaphy.2009.05.009 }}</ref>  Three-dimensional [[protein structure]]s of the peroxidated catalase intermediates are available at the [[Protein Data Bank]].
[[Arsenate]] acts as an [[Enzyme activator|activator]].<ref>{{cite journal | vauthors = Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ | title = Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure | journal = Plant Physiology and Biochemistry | volume = 47 | issue = 10 | pages = 960–5 | date = October 2009 | pmid = 19574057 | doi = 10.1016/j.plaphy.2009.05.009 }}</ref>  Three-dimensional [[protein structure]]s of the peroxidated catalase intermediates are available at the [[Protein Data Bank]].


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Hydrogen peroxide is a harmful byproduct of many normal [[metabolism|metabolic]] processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the [[Chemical decomposition|decomposition]] of hydrogen peroxide into less-reactive [[gas]]eous [[oxygen]] and water molecules.<ref name=Gaetani_1996>{{cite journal | vauthors = Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN | title = Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes | journal = Blood | volume = 87 | issue = 4 | pages = 1595–9 | date = February 1996 | pmid = 8608252 }}</ref>
Hydrogen peroxide is a harmful byproduct of many normal [[metabolism|metabolic]] processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the [[Chemical decomposition|decomposition]] of hydrogen peroxide into less-reactive [[gas]]eous [[oxygen]] and water molecules.<ref name=Gaetani_1996>{{cite journal | vauthors = Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN | title = Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes | journal = Blood | volume = 87 | issue = 4 | pages = 1595–9 | date = February 1996 | pmid = 8608252 }}</ref>


Mice genetically engineered to lack catalase are initially phenotypically normal.,<ref name=Ho_2004>{{cite journal | vauthors = Ho YS, Xiong Y, Ma W, Spector A, Ho DS | title = Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury | journal = The Journal of Biological Chemistry | volume = 279 | issue = 31 | pages = 32804–12 | date = July 2004 | pmid = 15178682 | doi = 10.1074/jbc.M404800200 }}</ref> however, catalase deficiency in mice may increase the likelihood of developing [[obesity]], fatty liver,<ref name="pmid27939935">{{cite journal | vauthors = Heit C, Marshall S, Singh S, Yu X, Charkoftaki G, Zhao H, Orlicky DJ, Fritz KS, Thompson DC, Vasiliou V | title = Catalase deletion promotes prediabetic phenotype in mice | journal = Free Radical Biology & Medicine | volume = 103 | issue = | pages = 48–56 | year = 2017 | pmid = 27939935 | doi = 10.1016/j.freeradbiomed.2016.12.011 | url = }}</ref> and [[Diabetes mellitus type 2|type 2 diabetes]].<ref name="Góth_2012">{{cite journal | vauthors = Góth L, Nagy T | title = Acatalasemia and diabetes mellitus | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 195–200 | year = 2012 | pmid = 22365890 | doi = 10.1016/j.abb.2012.02.005 }}</ref> Some humans have very low levels of catalase ([[acatalasia]]), yet show few ill effects.
Mice genetically engineered to lack catalase are initially phenotypically normal.,<ref name=Ho_2004>{{cite journal | vauthors = Ho YS, Xiong Y, Ma W, Spector A, Ho DS | title = Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury | journal = The Journal of Biological Chemistry | volume = 279 | issue = 31 | pages = 32804–12 | date = July 2004 | pmid = 15178682 | doi = 10.1074/jbc.M404800200 }}</ref> however, catalase deficiency in mice may increase the likelihood of developing [[obesity]], fatty liver,<ref name="pmid27939935">{{cite journal | vauthors = Heit C, Marshall S, Singh S, Yu X, Charkoftaki G, Zhao H, Orlicky DJ, Fritz KS, Thompson DC, Vasiliou V | title = Catalase deletion promotes prediabetic phenotype in mice | journal = Free Radical Biology & Medicine | volume = 103 | issue = | pages = 48–56 | year = 2017 | pmid = 27939935 | doi = 10.1016/j.freeradbiomed.2016.12.011 | pmc=5513671}}</ref> and [[Diabetes mellitus type 2|type 2 diabetes]].<ref name="Góth_2012">{{cite journal | vauthors = Góth L, Nagy T | title = Acatalasemia and diabetes mellitus | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 195–200 | year = 2012 | pmid = 22365890 | doi = 10.1016/j.abb.2012.02.005 }}</ref> Some humans have very low levels of catalase ([[acatalasia]]), yet show few ill effects.
 
The increased [[oxidative stress]] that occurs with [[ageing|aging]] in mice is alleviated by [[gene expression|over-expression]] of catalase.<ref name="pmid27575890">{{cite journal |vauthors=Selvaratnam J, Robaire B |title=Overexpression of catalase in mice reduces age-related oxidative stress and maintains sperm production |journal=Exp. Gerontol. |volume=84 |issue= |pages=12–20 |date=November 2016 |pmid=27575890 |doi=10.1016/j.exger.2016.08.012 |url=}}</ref>  Over-expressing mice do not exhibit the age-associated loss of [[spermatozoon|spermatozoa]], [[testicle|testicular]] [[germ cell|germ]] and [[Sertoli cell]]s seen in wild-type mice.  Oxidative stress in [[wild-type]] mice ordinarily induces oxidative [[DNA damage (naturally occurring)|DNA damage]] (measured as [[8-Oxo-2'-deoxyguanosine|8-oxodG]]) in [[sperm]] with aging, but these damages are significantly reduced in aged catalase over-expressing mice.<ref name="pmid27575890" />  Furthermore, these over-expressing mice show no decrease in age-dependent number of pups per litter.  Overexpression of catalase targeted to mitochondria extends the lifespan of mice.<ref name="pmid15879174">{{cite journal |vauthors=Schriner SE, Linford NJ, Martin GM, Treuting P, Ogburn CE, Emond M, Coskun PE, Ladiges W, Wolf N, Van Remmen H, Wallace DC, Rabinovitch PS |title=Extension of murine life span by overexpression of catalase targeted to mitochondria |journal=Science |volume=308 |issue=5730 |pages=1909–11 |date=June 2005 |pmid=15879174 |doi=10.1126/science.1106653 |url=|bibcode=2005Sci...308.1909S }}</ref>


Catalase is usually located in a cellular [[organelle]] called the [[peroxisome]].<ref name="MBOC">{{cite book |vauthors=Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Molecular Biology of the Cell | edition = 4th | publisher = Garland Science | location = New York | year = 2002 | origyear = | pages = | chapter = Peroxisomes | chapterurl = https://www.ncbi.nlm.nih.gov/books/NBK26858/ | quote = | isbn = 978-0-8153-3218-3 }}</ref> Peroxisomes in plant cells are involved in [[photorespiration]] (the use of oxygen and production of carbon dioxide) and symbiotic [[nitrogen fixation]] (the breaking apart of [[diatomic]] [[nitrogen]] (N<sub>2</sub>) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as ''[[Mycobacterium tuberculosis]]'', ''[[Legionella pneumophila]]'', and ''[[Campylobacter jejuni]]'', make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the [[Host (biology)|host]].<ref name="pmid12949187">{{cite journal | vauthors = Srinivasa Rao PS, Yamada Y, Leung KY | title = A major catalase (KatB) that is required for resistance to H2O2 and phagocyte-mediated killing in Edwardsiella tarda | journal = Microbiology | volume = 149 | issue = Pt 9 | pages = 2635–44 | date = September 2003 | pmid = 12949187 | doi = 10.1099/mic.0.26478-0 }}</ref>
Catalase is usually located in a cellular [[organelle]] called the [[peroxisome]].<ref name="MBOC">{{cite book |vauthors=Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P | title = Molecular Biology of the Cell | edition = 4th | publisher = Garland Science | location = New York | year = 2002 | origyear = | pages = | chapter = Peroxisomes | chapterurl = https://www.ncbi.nlm.nih.gov/books/NBK26858/ | quote = | isbn = 978-0-8153-3218-3 }}</ref> Peroxisomes in plant cells are involved in [[photorespiration]] (the use of oxygen and production of carbon dioxide) and symbiotic [[nitrogen fixation]] (the breaking apart of [[diatomic]] [[nitrogen]] (N<sub>2</sub>) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as ''[[Mycobacterium tuberculosis]]'', ''[[Legionella pneumophila]]'', and ''[[Campylobacter jejuni]]'', make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the [[Host (biology)|host]].<ref name="pmid12949187">{{cite journal | vauthors = Srinivasa Rao PS, Yamada Y, Leung KY | title = A major catalase (KatB) that is required for resistance to H2O2 and phagocyte-mediated killing in Edwardsiella tarda | journal = Microbiology | volume = 149 | issue = Pt 9 | pages = 2635–44 | date = September 2003 | pmid = 12949187 | doi = 10.1099/mic.0.26478-0 }}</ref>
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== Distribution among organisms ==
== Distribution among organisms ==
The large majority of known organisms use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]] in mammals.<ref>{{cite journal| vauthors = Ilyukha VA | journal=Journal of Evolutionary Biochemistry and Physiology | title = Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis |date=2001|volume=37|issue=3|pages=241–245|doi=10.1023/A:1012663105999}}</ref> One unique use of catalase occurs in the [[bombardier beetle]]. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.<ref name="pmid10449758">{{cite journal | vauthors = Eisner T, Aneshansley DJ | title = Spray aiming in the bombardier beetle: photographic evidence | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 17 | pages = 9705–9 | date = August 1999 | pmid = 10449758 | pmc = 22274 | doi = 10.1073/pnas.96.17.9705 | bibcode = 1999PNAS...96.9705E }}</ref> The oxidation reaction is very [[exothermic]] (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.<ref name="Beheshti_2006">{{cite journal | vauthors = Beheshti N, McIntosh AC | journal = Int. Journal of Design & Nature | year = 2006 | volume = 1 | issue = 1 | pages = 1–9 | url = http://www.heveliusforum.org/Artykuly/Biomimetics.pdf | title = A biomimetic study of the explosive discharge of the bombardier beetle | deadurl = yes | archiveurl = https://web.archive.org/web/20110726145856/http://www.heveliusforum.org/Artykuly/Biomimetics.pdf | archivedate = 2011-07-26 }}</ref>
The large majority of known organisms use catalase in every [[organ (anatomy)|organ]], with particularly high concentrations occurring in the [[liver]] in mammals.<ref>{{cite journal| vauthors = Ilyukha VA | journal=Journal of Evolutionary Biochemistry and Physiology | title = Superoxide Dismutase and Catalase in the Organs of Mammals of Different Ecogenesis |date=2001|volume=37|issue=3|pages=241–245|doi=10.1023/A:1012663105999}}</ref>Almost all [[aerobic microorganisms]] use catalase. It is also present in some [[Anaerobic organism|anaerobic]] [[microorganisms]], such as ''[[Methanosarcina barkeri]]''.<ref name="pmid16735730">{{cite journal | vauthors = Brioukhanov AL, Netrusov AI, Eggen RI | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri | journal = Microbiology | volume = 152 | issue = Pt 6 | pages = 1671–7 | date = June 2006 | pmid = 16735730 | doi = 10.1099/mic.0.28542-0 }}</ref> Catalase is also universal among [[plants]] and occurs in most [[fungi]].<ref>{{cite journal | vauthors = Hansberg W, Salas-Lizana R, Domínguez L | title = Fungal catalases: function, phylogenetic origin and structure | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 170–80 | date = September 2012 | pmid = 22698962 | doi = 10.1016/j.abb.2012.05.014 }}</ref>
 
One unique use of catalase occurs in the [[bombardier beetle]]. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains [[hydroquinone]]s and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and [[peroxidase]]s. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.<ref name="pmid10449758">{{cite journal|vauthors=Eisner T, Aneshansley DJ|date=August 1999|title=Spray aiming in the bombardier beetle: photographic evidence|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=96|issue=17|pages=9705–9|bibcode=1999PNAS...96.9705E|doi=10.1073/pnas.96.17.9705|pmc=22274|pmid=10449758}}</ref> The oxidation reaction is very [[exothermic]] (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.<ref name="Beheshti_2006">{{cite journal|vauthors=Beheshti N, McIntosh AC|year=2006|title=A biomimetic study of the explosive discharge of the bombardier beetle|url=http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|deadurl=yes|journal=Int. Journal of Design & Nature|volume=1|issue=1|pages=1–9|archiveurl=https://web.archive.org/web/20110726145856/http://www.heveliusforum.org/Artykuly/Biomimetics.pdf|archivedate=2011-07-26}}</ref>


Almost all [[aerobic microorganisms]] use catalase. It is also present in some [[Anaerobic organism|anaerobic]] [[microorganisms]], such as ''[[Methanosarcina barkeri]]''.<ref name="pmid16735730">{{cite journal | vauthors = Brioukhanov AL, Netrusov AI, Eggen RI | title = The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri | journal = Microbiology | volume = 152 | issue = Pt 6 | pages = 1671–7 | date = June 2006 | pmid = 16735730 | doi = 10.1099/mic.0.28542-0 }}</ref> Catalase is also universal among [[plants]] and occurs in most [[fungi]].<ref>{{cite journal | vauthors = Hansberg W, Salas-Lizana R, Domínguez L | title = Fungal catalases: function, phylogenetic origin and structure | journal = Archives of Biochemistry and Biophysics | volume = 525 | issue = 2 | pages = 170–80 | date = September 2012 | pmid = 22698962 | doi = 10.1016/j.abb.2012.05.014 }}</ref>
Long-lived queens of the [[termite]] ''[[Reticulitermes]] speratus'' have significantly lower [[DNA oxidation|oxidative damage to their DNA]] than non-reproductive individuals (workers and soldiers).<ref name="pmid28076409">{{cite journal |vauthors=Tasaki E, Kobayashi K, Matsuura K, Iuchi Y |title=An Efficient Antioxidant System in a Long-Lived Termite Queen |journal=PLoS ONE |volume=12 |issue=1 |pages=e0167412 |date=2017 |pmid=28076409 |pmc=5226355 |doi=10.1371/journal.pone.0167412 |url=|bibcode=2017PLoSO..1267412T }}</ref> Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.<ref name="pmid28076409" />  It appears that the efficient [[antioxidant]] capability of termite queens can partly explain how they attain longer life.


Catalase enzymes from various species have vastly differing optimum temperatures. [[Poikilotherm]]ic animals typically have catalases with optimum temperatures in the range of 15-25&nbsp;°C, while mammalian or avian catalases might have optimum temperatures above 35&nbsp;°C,<ref name="mits56" /><ref name="imm03">{{cite journal|last1=Akkuş Çetinus|first1=Şenay|last2=Nursevin Öztop|first2=H. | name-list-format = vanc |title=Immobilization of catalase into chemically crosslinked chitosan beads|journal=Enzyme and Microbial Technology|date=June 2003|volume=32|issue=7|pages=889–894|doi=10.1016/S0141-0229(03)00065-6}}</ref> and catalases from plants vary depending on their [[growth habit]].<ref name="mits56">{{cite journal|last1=Mitsuda|first1=Hisateru|title=Studies on Catalase|journal=Bulletin of the Institute for Chemical Research, Kyoto University|date=1956-07-31|volume=34|issue=4|pages=165–192|url=https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf|accessdate=27 September 2017}}</ref> In contrast, catalase isolated from the [[hyperthermophile]] [[archaeon]] ''[[Pyrobaculum calidifontis]]'' has a temperature optimum of 90&nbsp;°C.<ref name="pmid12029047">{{cite journal | vauthors = Amo T, Atomi H, Imanaka T | title = Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 | journal = Journal of Bacteriology | volume = 184 | issue = 12 | pages = 3305–12 | date = June 2002 | pmid = 12029047 | pmc = 135111 | doi = 10.1128/JB.184.12.3305-3312.2002 }}</ref>
Catalase enzymes from various species have vastly differing optimum temperatures. [[Poikilotherm]]ic animals typically have catalases with optimum temperatures in the range of 15-25&nbsp;°C, while mammalian or avian catalases might have optimum temperatures above 35&nbsp;°C,<ref name="mits56" /><ref name="imm03">{{cite journal|last1=Akkuş Çetinus|first1=Şenay|last2=Nursevin Öztop|first2=H. | name-list-format = vanc |title=Immobilization of catalase into chemically crosslinked chitosan beads|journal=Enzyme and Microbial Technology|date=June 2003|volume=32|issue=7|pages=889–894|doi=10.1016/S0141-0229(03)00065-6}}</ref> and catalases from plants vary depending on their [[growth habit]].<ref name="mits56">{{cite journal|last1=Mitsuda|first1=Hisateru|title=Studies on Catalase|journal=Bulletin of the Institute for Chemical Research, Kyoto University|date=1956-07-31|volume=34|issue=4|pages=165–192|url=https://repository.kulib.kyoto-u.ac.jp/dspace/bitstream/2433/75561/1/chd034_4_165.pdf|accessdate=27 September 2017}}</ref> In contrast, catalase isolated from the [[hyperthermophile]] [[archaeon]] ''[[Pyrobaculum calidifontis]]'' has a temperature optimum of 90&nbsp;°C.<ref name="pmid12029047">{{cite journal | vauthors = Amo T, Atomi H, Imanaka T | title = Unique presence of a manganese catalase in a hyperthermophilic archaeon, Pyrobaculum calidifontis VA1 | journal = Journal of Bacteriology | volume = 184 | issue = 12 | pages = 3305–12 | date = June 2002 | pmid = 12029047 | pmc = 135111 | doi = 10.1128/JB.184.12.3305-3312.2002 }}</ref>
Line 102: Line 104:
=== Bacterial virulence ===
=== Bacterial virulence ===
[[Neutrophil]]s and other [[phagocyte]]s use peroxide to kill bacteria. The enzyme [[NADPH oxidase]] generates [[superoxide]] within the [[phagosome]], which is converted via hydrogen peroxide to other oxidising substances like [[hypochlorous acid]] which kill [[phagocytosed]] pathogens.<ref>{{Cite journal|last=Winterbourn|first=Christine C.|last2=Kettle|first2=Anthony J.|last3=Hampton|first3=Mark B.|date=2016-06-02|title=Reactive Oxygen Species and Neutrophil Function|url=http://www.annualreviews.org/doi/10.1146/annurev-biochem-060815-014442|journal=Annual Review of Biochemistry|volume=85|issue=1|pages=765–792|doi=10.1146/annurev-biochem-060815-014442|issn=0066-4154}}</ref> In individuals with [[chronic granulomatous disease]] (CGD) there is a defect in producing peroxide via mutations in phagocyte oxidases such as [[myeloperoxidase]].<ref>{{Cite book|url=https://books.google.com/books?id=1NzVBQAAQBAJ&pg=PA169|title=The Neutrophil|last=Murphy|first=Patrick|date=2012-12-06|publisher=Springer Science & Business Media|isbn=9781468474183|language=en}}</ref> Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a [[granuloma]]. Many bacteria are catalase positive, but some are better catalase-producers than others. The mnemonic "cats Need PLACESS to Belch their Hairballs" can be used to memorise the catalase-positive bacteria: [[nocardia]], [[pseudomonas]], [[listeria]], [[aspergillus]], [[Candida albicans|candida]], [[Escherichia coli|E. coli]], [[staphylococcus]], [[serratia]], [[Burkholderia cepacia complex|B. cepacia]] and [[Helicobacter pylori|H. pylori]].<ref>{{Cite book|url=https://www.worldcat.org/oclc/986222844|title=First aid for the USMLE step 1 2017 : a student-to-student guide|others=Le, Tao,, Bhushan, Vikas,, Sochat, Matthew,, Kallianos, Kimberly,, Chavda, Yash,, Zureick, Andrew H. (Andrew Harrison), 1991-|isbn=9781259837623|edition=27th|location=New York|oclc=986222844}}</ref>
[[Neutrophil]]s and other [[phagocyte]]s use peroxide to kill bacteria. The enzyme [[NADPH oxidase]] generates [[superoxide]] within the [[phagosome]], which is converted via hydrogen peroxide to other oxidising substances like [[hypochlorous acid]] which kill [[phagocytosed]] pathogens.<ref>{{Cite journal|last=Winterbourn|first=Christine C.|last2=Kettle|first2=Anthony J.|last3=Hampton|first3=Mark B.|date=2016-06-02|title=Reactive Oxygen Species and Neutrophil Function|url=http://www.annualreviews.org/doi/10.1146/annurev-biochem-060815-014442|journal=Annual Review of Biochemistry|volume=85|issue=1|pages=765–792|doi=10.1146/annurev-biochem-060815-014442|issn=0066-4154}}</ref> In individuals with [[chronic granulomatous disease]] (CGD) there is a defect in producing peroxide via mutations in phagocyte oxidases such as [[myeloperoxidase]].<ref>{{Cite book|url=https://books.google.com/books?id=1NzVBQAAQBAJ&pg=PA169|title=The Neutrophil|last=Murphy|first=Patrick|date=2012-12-06|publisher=Springer Science & Business Media|isbn=9781468474183|language=en}}</ref> Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a [[granuloma]]. Many bacteria are catalase positive, but some are better catalase-producers than others. The mnemonic "cats Need PLACESS to Belch their Hairballs" can be used to memorise the catalase-positive bacteria: [[nocardia]], [[pseudomonas]], [[listeria]], [[aspergillus]], [[Candida albicans|candida]], [[Escherichia coli|E. coli]], [[staphylococcus]], [[serratia]], [[Burkholderia cepacia complex|B. cepacia]] and [[Helicobacter pylori|H. pylori]].<ref>{{Cite book|url=https://www.worldcat.org/oclc/986222844|title=First aid for the USMLE step 1 2017 : a student-to-student guide|others=Le, Tao,, Bhushan, Vikas,, Sochat, Matthew,, Kallianos, Kimberly,, Chavda, Yash,, Zureick, Andrew H. (Andrew Harrison), 1991-|isbn=9781259837623|edition=27th|location=New York|oclc=986222844}}</ref>
=== Acatalasia ===
[[Acatalasia]] is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include oral ulcers. A heterozygous CAT mutation results in lower, but still present catalase.<ref>{{cite web |title=OMIM Entry            - # 614097 - ACATALASEMIA |url=http://www.omim.org/entry/614097 |website=www.omim.org |language=en-us}}</ref>


=== Gray hair ===
=== Gray hair ===
Low levels of catalase may play a role in the [[Human hair color#Gray and white hair|graying]] process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide cannot be broken down so well. The hydrogen peroxide interferes with the production of [[melanin]], the pigment that gives hair its color.<ref name="ScienceDaily_Grey_Hair">{{cite web | url = http://www.sciencedaily.com/releases/2009/02/090223131123.htm | title = Why Hair Turns Gray Is No Longer A Gray Area: Our Hair Bleaches Itself As We Grow Older | date = 2009-02-24 | work = Science News | publisher = ScienceDaily | accessdate = 2009-03-01}}</ref><ref name="pmid19237503">{{cite journal | vauthors = Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton MJ, Shalbaf M, Paus R, Schallreuter KU | title = Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair | journal = FASEB Journal | volume = 23 | issue = 7 | pages = 2065–75 | date = July 2009 | pmid = 19237503 | doi = 10.1096/fj.08-125435 }}</ref>
Low levels of catalase may play a role in the [[Human hair color#Gray and white hair|graying]] process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide cannot be broken down so well. The hydrogen peroxide interferes with the production of [[melanin]], the pigment that gives hair its color.<ref name="ScienceDaily_Grey_Hair">{{cite web | url = https://www.sciencedaily.com/releases/2009/02/090223131123.htm | title = Why Hair Turns Gray Is No Longer A Gray Area: Our Hair Bleaches Itself As We Grow Older | date = 2009-02-24 | work = Science News | publisher = ScienceDaily | accessdate = 2009-03-01}}</ref><ref name="pmid19237503">{{cite journal | vauthors = Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton MJ, Shalbaf M, Paus R, Schallreuter KU | title = Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair | journal = FASEB Journal | volume = 23 | issue = 7 | pages = 2065–75 | date = July 2009 | pmid = 19237503 | doi = 10.1096/fj.08-125435 }}</ref>


== Interactions ==
== Interactions ==
Line 112: Line 117:
== See also ==
== See also ==
* [[Enzyme kinetics]]
* [[Enzyme kinetics]]
* [[Peroxidases]]
* [[Glutathione peroxidase]]
* [[Peroxidase]]
* [[Superoxide dismutase]]
* [[Superoxide dismutase]]


Latest revision as of 18:30, 2 January 2019

Catalase
File:PDB 7cat EBI.jpg
Identifiers
SymbolCatalase
PfamPF00199
InterProIPR011614
PROSITEPDOC00395
SCOP7cat
SUPERFAMILY7cat
OPM superfamily370
OPM protein3e4w
CDDcd00328
Catalase
Identifiers
EC number1.11.1.6
CAS number9001-05-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen.[1] It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.[2]

Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.[3] It contains four iron-containing heme groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for human catalase is approximately 7,[4] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.[5] The pH optimum for other catalases varies between 4 and 11 depending on the species.[6] The optimum temperature also varies by species.[7]

Structure

Human catalase forms a tetramer composed of four subunits, each of which can be conceptually divided into four domains.[8] The extensive core of each subunit is generated by an eight-stranded antiparallel b-barrel (b1-8), with nearest neighbor connectivity capped by b-barrel loops on one side and a9 loops on the other.[8] A helical domain at one face of the b-barrel is composed of four C-terminal helices (a16, a17, a18, and a19) and four helices derived from residues between b4 and b5 (a4, a5, a6, and a7).[8] Alternative splicing may result in different protein variants.

History

Catalase was not noticed until 1818 when Louis Jacques Thénard, who discovered H2O2 (hydrogen peroxide), suggested its breakdown is caused by an unknown substance. In 1900, Oscar Loew was the first to give it the name catalase, and found it in many plants and animals.[9] In 1937 catalase from beef liver was crystallised by James B. Sumner and Alexander Dounce[10] and the molecular weight was found in 1938.[11]

The amino acid sequence of bovine catalase was determined in 1969,[12] and the three-dimensional structure in 1981.[13]

Function

Reaction

2 H2O2 → 2 H2O + O2

The presence of catalase in a microbial or tissue sample can be demonstrated by adding hydrogen peroxide and observing the reaction. The production of oxygen can be seen by the formation of bubbles. This easy test, which can be seen with the naked eye, without the aid of instruments, is possible because catalase has a very high specific activity, which produces a detectable response, as well as the fact that one of the products is a gas.

Molecular mechanism

While the complete mechanism of catalase is not currently known,[14] the reaction is believed to occur in two stages:

H2O2 + Fe(III)-E → H2O + O=Fe(IV)-E(.+)
H2O2 + O=Fe(IV)-E(.+) → H2O + Fe(III)-E + O2[14]

Here Fe()-E represents the iron center of the heme group attached to the enzyme. Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning the iron is not completely oxidized to +V, but receives some stabilising electron density from the heme ligand, which is then shown as a radical cation (.+).

As hydrogen peroxide enters the active site, it interacts with the amino acids Asn148 (asparagine at position 148) and His75, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to reform Fe(III)-E and produce water and oxygen.[14] The reactivity of the iron center may be improved by the presence of the phenolate ligand of Tyr358 in the fifth coordination position, which can assist in the oxidation of the Fe(III) to Fe(IV). The efficiency of the reaction may also be improved by the interactions of His75 and Asn148 with reaction intermediates.[14] In general, the rate of the reaction can be determined by the Michaelis-Menten equation.[15]

Catalase can also catalyze the oxidation, by hydrogen peroxide, of various metabolites and toxins, including formaldehyde, formic acid, phenols, acetaldehyde and alcohols. It does so according to the following reaction:

H2O2 + H2R → 2H2O + R

The exact mechanism of this reaction is not known.

Any heavy metal ion (such as copper cations in copper(II) sulfate) can act as a noncompetitive inhibitor of catalase. Furthermore, the poison cyanide is a noncompetitive inhibitor[16] of catalase at high concentrations of hydrogen peroxide.[17] Arsenate acts as an activator.[18] Three-dimensional protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank.

Cellular role

Hydrogen peroxide is a harmful byproduct of many normal metabolic processes; to prevent damage to cells and tissues, it must be quickly converted into other, less dangerous substances. To this end, catalase is frequently used by cells to rapidly catalyze the decomposition of hydrogen peroxide into less-reactive gaseous oxygen and water molecules.[19]

Mice genetically engineered to lack catalase are initially phenotypically normal.,[20] however, catalase deficiency in mice may increase the likelihood of developing obesity, fatty liver,[21] and type 2 diabetes.[22] Some humans have very low levels of catalase (acatalasia), yet show few ill effects.

The increased oxidative stress that occurs with aging in mice is alleviated by over-expression of catalase.[23] Over-expressing mice do not exhibit the age-associated loss of spermatozoa, testicular germ and Sertoli cells seen in wild-type mice. Oxidative stress in wild-type mice ordinarily induces oxidative DNA damage (measured as 8-oxodG) in sperm with aging, but these damages are significantly reduced in aged catalase over-expressing mice.[23] Furthermore, these over-expressing mice show no decrease in age-dependent number of pups per litter. Overexpression of catalase targeted to mitochondria extends the lifespan of mice.[24]

Catalase is usually located in a cellular organelle called the peroxisome.[25] Peroxisomes in plant cells are involved in photorespiration (the use of oxygen and production of carbon dioxide) and symbiotic nitrogen fixation (the breaking apart of diatomic nitrogen (N2) to reactive nitrogen atoms). Hydrogen peroxide is used as a potent antimicrobial agent when cells are infected with a pathogen. Catalase-positive pathogens, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, make catalase to deactivate the peroxide radicals, thus allowing them to survive unharmed within the host.[26]

Like alcohol dehydrogenase, catalase converts ethanol to acetaldehyde, but it is unlikely that this reaction is physiologically significant.[27]

Distribution among organisms

The large majority of known organisms use catalase in every organ, with particularly high concentrations occurring in the liver in mammals.[28]Almost all aerobic microorganisms use catalase. It is also present in some anaerobic microorganisms, such as Methanosarcina barkeri.[29] Catalase is also universal among plants and occurs in most fungi.[30]

One unique use of catalase occurs in the bombardier beetle. This beetle has two sets of liquids that are stored separately in two paired glands. The larger of the pair, the storage chamber or reservoir, contains hydroquinones and hydrogen peroxide, while the smaller, the reaction chamber, contains catalases and peroxidases. To activate the noxious spray, the beetle mixes the contents of the two compartments, causing oxygen to be liberated from hydrogen peroxide. The oxygen oxidizes the hydroquinones and also acts as the propellant.[31] The oxidation reaction is very exothermic (ΔH = −202.8 kJ/mol) and rapidly heats the mixture to the boiling point.[32]

Long-lived queens of the termite Reticulitermes speratus have significantly lower oxidative damage to their DNA than non-reproductive individuals (workers and soldiers).[33] Queens have more than two times higher catalase activity and seven times higher expression levels of the catalase gene RsCAT1 than workers.[33] It appears that the efficient antioxidant capability of termite queens can partly explain how they attain longer life.

Catalase enzymes from various species have vastly differing optimum temperatures. Poikilothermic animals typically have catalases with optimum temperatures in the range of 15-25 °C, while mammalian or avian catalases might have optimum temperatures above 35 °C,[34][35] and catalases from plants vary depending on their growth habit.[34] In contrast, catalase isolated from the hyperthermophile archaeon Pyrobaculum calidifontis has a temperature optimum of 90 °C.[36]

Clinical significance and application

Hydrogen peroxide

Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production.[37] Another use is in food wrappers where it prevents food from oxidizing.[38] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free.[39]

A minor use is in contact lens hygiene – a few lens-cleaning products disinfect the lens using a hydrogen peroxide solution; a solution containing catalase is then used to decompose the hydrogen peroxide before the lens is used again.[40]

Bacterial identification (catalase test)

File:Catalase reaction.jpg
Positive catalase reaction

The catalase test is one of the three main tests used by microbiologists to identify species of bacteria. If the bacteria possess catalase (i.e., are catalase-positive), when a small amount of bacterial isolate is added to hydrogen peroxide, bubbles of oxygen are observed. The catalase test is done by placing a drop of hydrogen peroxide on a microscope slide. An applicator stick is touched to the colony, and the tip is then smeared onto the hydrogen peroxide drop.

While the catalase test alone cannot identify a particular organism, it can aid identification when combined with other tests such as antibiotic resistance. The presence of catalase in bacterial cells depends on both the growth condition and the medium used to grow the cells.

Capillary tubes may also be used. A small sample of bacteria is collected on the end of the capillary tube, without blocking the tube, to avoid false negative results. The opposite end is then dipped into hydrogen peroxide, which is drawn into the tube through capillary action, and turned upside down, so that the bacterial points downwards. The hand holding the tube is then tapped on the bench, moving the hydrogen peroxide down until it touches the bacteria. If bubbles form on contact, this indicates a positive catalase result. This test can detect catalase-positive bacteria at concentrations above about 105 cells/mL,[44] and is simple to use.

Bacterial virulence

Neutrophils and other phagocytes use peroxide to kill bacteria. The enzyme NADPH oxidase generates superoxide within the phagosome, which is converted via hydrogen peroxide to other oxidising substances like hypochlorous acid which kill phagocytosed pathogens.[45] In individuals with chronic granulomatous disease (CGD) there is a defect in producing peroxide via mutations in phagocyte oxidases such as myeloperoxidase.[46] Normal cellular metabolism will still produce a small amount of peroxide and this peroxide can be used to produce hypochlorous acid to eradicate the bacterial infection. However, if individuals with CGD are infected with catalase-positive bacteria, the bacterial catalase can destroy the excess peroxide before it can be used to produce other oxidising substances. In these individuals the pathogen survives and becomes a chronic infection. This chronic infection is typically surrounded by macrophages in an attempt to isolate the infection. This wall of macrophages surrounding a pathogen is called a granuloma. Many bacteria are catalase positive, but some are better catalase-producers than others. The mnemonic "cats Need PLACESS to Belch their Hairballs" can be used to memorise the catalase-positive bacteria: nocardia, pseudomonas, listeria, aspergillus, candida, E. coli, staphylococcus, serratia, B. cepacia and H. pylori.[47]

Acatalasia

Acatalasia is a condition caused by homozygous mutations in CAT, resulting in a lack of catalase. Symptoms are mild and include oral ulcers. A heterozygous CAT mutation results in lower, but still present catalase.[48]

Gray hair

Low levels of catalase may play a role in the graying process of human hair. Hydrogen peroxide is naturally produced by the body and broken down by catalase. If catalase levels decline, hydrogen peroxide cannot be broken down so well. The hydrogen peroxide interferes with the production of melanin, the pigment that gives hair its color.[49][50]

Interactions

Catalase has been shown to interact with the ABL2[51] and Abl genes.[51] Infection with the murine leukemia virus causes catalase activity to decline in the lungs, heart and kidneys of mice. Conversely, dietary fish oil increased catalase activity in the heart, and kidneys of mice.[52]

See also

References

  1. ↑ Chelikani P, Fita I, Loewen PC (January 2004). "Diversity of structures and properties among catalases". Cellular and Molecular Life Sciences. 61 (2): 192–208. doi:10.1007/s00018-003-3206-5. PMID 14745498.
  2. ↑ Goodsell DS (2004-09-01). "Catalase". Molecule of the Month. RCSB Protein Data Bank. Retrieved 2016-08-23.
  3. ↑ Boon EM, Downs A, Marcey D. "Catalase: H2O2: H2O2 Oxidoreductase". Catalase Structural Tutorial Text. Retrieved 2007-02-11.
  4. ↑ Maehly AC, Chance B (1954). "The assay of catalases and peroxidases". Methods of Biochemical Analysis. Methods of Biochemical Analysis. 1: 357–424. doi:10.1002/9780470110171.ch14. ISBN 978-0-470-11017-1. PMID 13193536.
  5. ↑ Aebi H (1984). "Catalase in vitro". Methods in Enzymology. Methods in Enzymology. 105: 121–6. doi:10.1016/S0076-6879(84)05016-3. ISBN 978-0-12-182005-3. PMID 6727660.
  6. ↑ "EC 1.11.1.6 - catalase". BRENDA: The Comprehensive Enzyme Information System. Department of Bioinformatics and Biochemistry, Technische Universität Braunschweig. Retrieved 2009-05-26.
  7. ↑ Toner K, Sojka G, Ellis R. "A Quantitative Enzyme Study; CATALASE". bucknell.edu. Archived from the original on 2000-06-12. Retrieved 2007-02-11.
  8. ↑ 8.0 8.1 8.2 Putnam CD, Arvai AS, Bourne Y, Tainer JA (February 2000). "Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism". Journal of Molecular Biology. 296 (1): 295–309. doi:10.1006/jmbi.1999.3458. PMID 10656833.
  9. ↑ Loew O (May 1900). "A New Enzyme of General Occurrence in Organisms". Science. 11 (279): 701–2. Bibcode:1900Sci....11..701L. doi:10.1126/science.11.279.701. JSTOR 1625707. PMID 17751716.
  10. ↑ Sumner JB, Dounce AL (April 1937). "Crystalline Catalase". Science. 85 (2206): 366–7. Bibcode:1937Sci....85..366S. doi:10.1126/science.85.2206.366. PMID 17776781.
  11. ↑ Sumner JB, Gralén N (March 1938). "The Molecular Weight Of Crystalline Catalase". Science. 87 (2256): 284. Bibcode:1938Sci....87..284S. doi:10.1126/science.87.2256.284. PMID 17831682.
  12. ↑ Schroeder WA, Shelton JR, Shelton JB, Robberson B, Apell G (May 1969). "The amino acid sequence of bovine liver catalase: a preliminary report". Archives of Biochemistry and Biophysics. 131 (2): 653–5. doi:10.1016/0003-9861(69)90441-X. PMID 4892021.
  13. ↑ Murthy MR, Reid TJ, Sicignano A, Tanaka N, Rossmann MG (October 1981). "Structure of beef liver catalase". Journal of Molecular Biology. 152 (2): 465–99. doi:10.1016/0022-2836(81)90254-0. PMID 7328661.
  14. ↑ 14.0 14.1 14.2 14.3 Boon EM, Downs A, Marcey D. "Proposed Mechanism of Catalase". Catalase: H2O2: H2O2 Oxidoreductase: Catalase Structural Tutorial. Retrieved 2007-02-11.
  15. ↑ Maass E (1998-07-19). "How does the concentration of hydrogen peroxide affect the reaction". MadSci Network. Retrieved 2009-03-02.
  16. ↑ Nonstationary Inhibition of Enzyme Action. The Cyanide Inhibition of Catalase
  17. ↑ Ogura Y, Yamazaki I (August 1983). "Steady-state kinetics of the catalase reaction in the presence of cyanide". Journal of Biochemistry. 94 (2): 403–8. doi:10.1093/oxfordjournals.jbchem.a134369. PMID 6630165.
  18. ↑ Kertulis-Tartar GM, Rathinasabapathi B, Ma LQ (October 2009). "Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure". Plant Physiology and Biochemistry. 47 (10): 960–5. doi:10.1016/j.plaphy.2009.05.009. PMID 19574057.
  19. ↑ Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN (February 1996). "Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes". Blood. 87 (4): 1595–9. PMID 8608252.
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