Phosphogluconate dehydrogenase: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m →References: deprecated parameter using AWB
 
imported>Me, Myself, and I are Here
m →top: bold
 
Line 47: Line 47:
|LocusSupplementaryData=-36.13
|LocusSupplementaryData=-36.13
}}
}}
'''6-Phosphogluconate dehydrogenase''' (6PGD) is an [[enzyme]] in the [[pentose phosphate pathway]]. It forms [[ribulose 5-phosphate]] from [[6-phosphogluconate]].
'''6-Phosphogluconate dehydrogenase''' ('''6PGD''') is an [[enzyme]] in the [[pentose phosphate pathway]]. It forms [[ribulose 5-phosphate]] from [[6-phosphogluconate]].


It is an oxidative carboxylase that [[catalysis|catalyses]] the decarboxylating [[Redox|reduction]] of [[6-phosphogluconate]] into [[ribulose 5-phosphate]] in the presence of [[NADP]]. This reaction is a component of the [[hexose]] mono-phosphate shunt and [[pentose phosphate pathway]]s (PPP).<ref name="pmid2113917">{{cite journal | vauthors = Broedel SE, Wolf RE | title = Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase | journal = J. Bacteriol. | volume = 172 | issue = 7 | pages = 4023–31 |date=July 1990 | pmid = 2113917 | pmc = 213388 | doi = | url = }}</ref><ref name="pmid6641716">{{cite journal | vauthors = Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW | title = The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution | journal = EMBO J. | volume = 2 | issue = 6 | pages = 1009–14 | year = 1983 | pmid = 6641716 | pmc = 555222 | doi = | url = }}</ref> [[Prokaryotic]] and [[eukaryotic]] 6PGD are [[protein]]s of about 470 [[amino acid]]s whose [[sequence (biology)|sequence]]s are [[Conservation (genetics)|highly conserved]].<ref name="pmid1659648">{{cite journal | vauthors = Reizer A, Deutscher J, Saier MH, Reizer J | title = Analysis of the gluconate (gnt) operon of Bacillus subtilis | journal = Mol. Microbiol. | volume = 5 | issue = 5 | pages = 1081–9 |date=May 1991 | pmid = 1659648 | doi = 10.1111/j.1365-2958.1991.tb01880.x| url = }}</ref> The protein is a [[homodimer]] in which the [[monomer]]s act independently:<ref name="pmid6641716" /> each contains a large, mainly [[alpha helix|alpha-helical]] [[Domain (biology)|domain]] and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded [[beta sheet]].<ref name="pmid6641716" /> NADP is bound in a cleft in the small domain, the [[Enzyme substrate|substrate]] [[Binding (molecular)|binding]] in an adjacent pocket.<ref name="pmid6641716" />
It is an oxidative carboxylase that [[catalysis|catalyses]] the decarboxylating [[Redox|reduction]] of [[6-phosphogluconate]] into [[ribulose 5-phosphate]] in the presence of [[NADP]]. This reaction is a component of the [[hexose]] mono-phosphate shunt and [[pentose phosphate pathway]]s (PPP).<ref name="pmid2113917">{{cite journal | vauthors = Broedel SE, Wolf RE | title = Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase | journal = J. Bacteriol. | volume = 172 | issue = 7 | pages = 4023–31 |date=July 1990 | pmid = 2113917 | pmc = 213388 | doi = | url = }}</ref><ref name="pmid6641716">{{cite journal | vauthors = Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW | title = The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution | journal = EMBO J. | volume = 2 | issue = 6 | pages = 1009–14 | year = 1983 | pmid = 6641716 | pmc = 555222 | doi = | url = }}</ref> [[Prokaryotic]] and [[eukaryotic]] 6PGD are [[protein]]s of about 470 [[amino acid]]s whose [[sequence (biology)|sequence]]s are [[Conservation (genetics)|highly conserved]].<ref name="pmid1659648">{{cite journal | vauthors = Reizer A, Deutscher J, Saier MH, Reizer J | title = Analysis of the gluconate (gnt) operon of Bacillus subtilis | journal = Mol. Microbiol. | volume = 5 | issue = 5 | pages = 1081–9 |date=May 1991 | pmid = 1659648 | doi = 10.1111/j.1365-2958.1991.tb01880.x| url = }}</ref> The protein is a [[homodimer]] in which the [[monomer]]s act independently:<ref name="pmid6641716" /> each contains a large, mainly [[alpha helix|alpha-helical]] [[Domain (biology)|domain]] and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded [[beta sheet]].<ref name="pmid6641716" /> NADP is bound in a cleft in the small domain, the [[Enzyme substrate|substrate]] [[Binding (molecular)|binding]] in an adjacent pocket.<ref name="pmid6641716" />

Latest revision as of 05:47, 6 January 2018

6PGD
File:PDB 1pgq EBI.jpg
Crystallographic structure of sheep 6-phosphogluconate dehydrogenase complexed with adenosine 2'-monophosphate.[1]
Identifiers
Symbol6PGD
PfamPF00393
Pfam clanCL0106
InterProIPR006114
PROSITEPDOC00390
SCOP2pgd
SUPERFAMILY2pgd
Phosphogluconate dehydrogenase
Identifiers
EC number1.1.1.44
CAS number9001-82-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
phosphogluconate dehydrogenase
Identifiers
SymbolPGD
Entrez5226
HUGO8891
OMIM172200
RefSeqNM_002631
UniProtP52209
Other data
EC number1.1.1.44
LocusChr. 1 p36.3-36.13

6-Phosphogluconate dehydrogenase (6PGD) is an enzyme in the pentose phosphate pathway. It forms ribulose 5-phosphate from 6-phosphogluconate.

It is an oxidative carboxylase that catalyses the decarboxylating reduction of 6-phosphogluconate into ribulose 5-phosphate in the presence of NADP. This reaction is a component of the hexose mono-phosphate shunt and pentose phosphate pathways (PPP).[2][3] Prokaryotic and eukaryotic 6PGD are proteins of about 470 amino acids whose sequences are highly conserved.[4] The protein is a homodimer in which the monomers act independently:[3] each contains a large, mainly alpha-helical domain and a smaller beta-alpha-beta domain, containing a mixed parallel and anti-parallel 6-stranded beta sheet.[3] NADP is bound in a cleft in the small domain, the substrate binding in an adjacent pocket.[3]

Clinical significance

Mutations within the gene coding this enzyme result in 6-phosphogluconate dehydrogenase deficiency, an autosomal hereditary disease affecting the red blood cells.

As a possible drug target

6PGD is involved in cancer cell metabolism so 6PGD inhibitors have been sought.[5]

See also

References

  1. ↑ PDB: 1PGQ​; Adams MJ, Ellis GH, Gover S, Naylor CE, Phillips C (July 1994). "Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism". Structure. 2 (7): 651–68. doi:10.1016/s0969-2126(00)00066-6. PMID 7922042.
  2. ↑ Broedel SE, Wolf RE (July 1990). "Genetic tagging, cloning, and DNA sequence of the Synechococcus sp. strain PCC 7942 gene (gnd) encoding 6-phosphogluconate dehydrogenase". J. Bacteriol. 172 (7): 4023–31. PMC 213388. PMID 2113917.
  3. ↑ 3.0 3.1 3.2 3.3 Adams MJ, Archibald IG, Bugg CE, Carne A, Gover S, Helliwell JR, Pickersgill RW, White SW (1983). "The three dimensional structure of sheep liver 6-phosphogluconate dehydrogenase at 2.6 A resolution". EMBO J. 2 (6): 1009–14. PMC 555222. PMID 6641716.
  4. ↑ Reizer A, Deutscher J, Saier MH, Reizer J (May 1991). "Analysis of the gluconate (gnt) operon of Bacillus subtilis". Mol. Microbiol. 5 (5): 1081–9. doi:10.1111/j.1365-2958.1991.tb01880.x. PMID 1659648.
  5. ↑ 6-Phosphogluconate dehydrogenase links oxidative PPP, lipogenesis and tumour growth by inhibiting LKB1–AMPK signalling. 2015
This article incorporates text from the public domain Pfam and InterPro: IPR006114

Template:Pentose phosphate pathway


Retrieved from "https://www.wikidoc.org/index.php?title=Phosphogluconate_dehydrogenase&oldid=1530346"