View source for Enoyl CoA isomerase

{{Infobox protein
|Name=Enoyl-CoA Isomerase
|caption=3,2-trans-enoyl-CoA isomerase trimer, Human
|image=1sg4.jpg
|width=270
|Symbol=DCI
|ECnumber=5.3.3.8
|UniProt=P42126
|DrugBank=DB03211
|Chromosome=16
|Arm=p
|Band=13.3
|LocusSupplementaryData=
}}
'''Enoyl-CoA-(∆) isomerase''', also known as '''dodecenoyl-CoA-(∆) isomerase''', '''3,2-trans-enoyl-CoA isomerase''', '''∆3(cis),∆2(trans)-enoyl-CoA isomerase''', or '''acetylene-allene isomerase''',<ref name="refname1" /> ({{EC number|5.3.3.8}}) is an [[enzyme]] that catalyzes the conversion of cis-or trans-[[double bond]]s of [[fatty acids]] at gamma-[[carbon]] (position 3) to trans [[double bond]]s at beta-[[carbon]] (position 2). It plays a particularly important role in the [[metabolism]] of [[unsaturated fatty acid]]s.

==Enzyme mechanism==
[[File:Reaction Mechanism of Enoyl-CoA Isomerase.pdf|thumb|Figure 1: Reaction Mechanism of Enoyl-CoA Isomerase]]

Enoyl-CoA [[isomerase]] is involved in the [[beta-oxidation]], one of the most frequently used pathways in [[fatty acid degradation]], of [[unsaturated fatty acid]]s with [[double bond]]s at odd-numbered [[carbon]] positions.<ref name="refname2" /> It does so by shifting the position of the [[double bond]]s in the acyl-CoA [[Reaction intermediate|intermediate]]s and converting 3-cis or trans-enoyl-CoA to 2-trans-enoyl-CoA. Since the key step in the degradation of [[fatty acids]] with [[double bond]]s at even-numbered [[carbon]] positions also produces 3-trans-enoyl-CoA in [[mammal]]s and [[yeast]]s, enoyl-CoA [[isomerase]] is technically required for their [[metabolism]] as well.<ref name="refname3" /> The [[reaction mechanism]] is detailed in Figure 1,<ref name="refname4" /> and the [[base (chemistry)|base]] that initiates the [[isomerization]] and NH groups that stabilize the [[Reaction intermediate|intermediate]] are located on the [[active site]] of enoyl-coA [[isomerase]].

As it functions in the step immediately preceding the actual [[beta-oxidation]] and forms a [[double bond]] extending from the beta-[[carbon]] (position 2), enoyl-CoA [[isomerase]] is involved in both the [[NADPH]]-dependent and [[NADPH]]-independent pathways of [[beta-oxidation]].<ref name="refname5" /> The [[double bond]] serves as the target of [[oxidation]] and [[carbon]]-to-[[carbon]] [[bond cleavage]], thereby shortening the [[fatty acid]] chain.

==Enzyme sub-classification==
Enoyl-CoA [[isomerases]] can be categorized into three classes:
* monofunctional [[mitochondrial]]
* monofunctional [[peroxisomal]]
* multifunctional
The monofunctional [[mitochondrial]] and [[peroxisomal]] [[enzyme]]s are found in the [[mitochondria]] and [[peroxisome]]s of [[eukaryote]]s, respectively. The multifunctional [[enzyme]]s are found in [[bacteria]] and in the [[peroxisome]]s of some [[eukaryote]]s, but they serve two functions: the [[N-terminal]] domain works the same as the other classes of enoyl-CoA [[isomerase]]s and the [[C-terminal]] domain works as a [[dehydrogenase]], specifically, to 3-hydroxyactyl-CoA.<ref name="refname4" /> There are two divisions among the [[mitochondria]]l enoyl Co-A isomerase: short-chain and long-chain [4].<ref name=refname20 /> In an immunoblot, antibodies were run against all enoyl CoA isomerase. However, two of these [[isomerase]]s had [[antibody]] attachment: the short chain isomerase and the peroxisomal multifunctional enzyme.<ref name=refname20 /> There was one [[enzyme]] which did not have binding specificity to this [[antibody]]: mitochondrial long-chain isomerase. Long-chain isomerase was found when it eluted at a lower potassium phosphate [[concentration]] in the gradient.<ref name=refname20 /><ref name=refname23 /> Thus, the discovery of three sub-classes of enoyl CoA isomerase was made.

Although all three classes of [[enzyme]]s have the same function, there is little overlap among their [[amino acid]] sequences. For example, only 40 out of 302 [[amino acid]] sequences (13%) are the same between monofunctional [[peroxisomal]] and [[mitochondrial]] [[enzyme]]s in [[human]]s.<ref name="refname4" /> In fact, in [[mammal]]s, the [[peroxisomal]] [[enzyme]] has an extra [[N-terminal]] domain that is not present in the [[mitochondrial]] counterpart.<ref name= "refname6" /> Also, it has been found to be a [[Protein subunit|subunit]] of the peroxisomal trifunctional [[enzyme]] (pTFE) and contributes only to minor cleavages of the [[fatty acid]] chain. In that sense, for many higher organisms, the [[mitochondrial]] [[enzyme]] is essential for deriving maximum [[energy]] from [[lipid]]s and fueling [[muscle]]s.<ref name="refname7" />

[[File:MFE or Isomerase.png|thumb|If the enzyme is unclear, react it with an enoyl CoA Derivative. If the enzyme gives off more than one product, it is a multifunctional enzyme. If it gives off one product, it is solely enoyl Co-Al isomerase.<ref name=refname21 />]]

[[Mitochondria]] (both short- and long-chain) of rat [[liver]] contain more than one enoyl Co-A isomerase.<ref name=refname21 /> To further support the idea that short- and long-chain isomerases elute at different concentration of potassium phosphate concentration, they do not share similar primary polypeptide structure, hence they must not be evolutionarily related.<ref name=refname20 /><ref name=refname17 /> [[Peroxisome]]s of [[plants]] and of rat [[liver]] are very different in the way they operate. Despite their [[primary structure]] similarities, there are differences among the different specimen. To begin with, the [[peroxisome]]s of rat [[liver]] are a multifunctional [[enzyme]] including enoyl-CoA isomerase, enoyl-CoA [[hydratase]], and L-(−)-3-hydroxyacyl-CoA [[dehydrogenase]].<ref name=refname26 /> Three different [[enzyme]]s reside on this entity (multifunctional protein) allowing this [[enzyme]] to perform isomerization, hydration, and dehydration.<ref name=refname18 /><ref name=refname27 /> Isomerase activity on the multifunctional [[enzyme]] occurs at the amino-terminal [[catalytic]] half of the protein along with the [[hydratase]] activity.<ref name=refname19 /> The [[dehydrogenase]] activity of enoyl-CoA occurs in the carboxyl-terminal.<ref name=refname19 /> Upon further investigation of the CoA [[binding site]] on the amino-terminal half of the multifunctional [[protein]], the CoA [[substrate (biochemistry)|substrate]] is not transferred through the aqueous phase from the isomerization phase to the site of hydration or does not have a bulk phase.<ref name=refname17 /><ref name=refname22 /> This removes the need for a substrate transferring [[enzyme]].<ref name=refname25 /> On the other hand, the [[cotyledon]]s convert long-chain 3-trans-enoyl-CoA, long-chain 3-cis-enoyl-CoA, and short-chain 3-cis-enoyl-CoA species into their 2- trans-enoyl-CoA respective forms.<ref name=refname18 /> As previously mentioned, [[plant]] enoyl-CoA isomerase exclusively forms the 2-trans [[isomer]] as [[product (biology)|product]]. It does not act on 4-cis-enoyl-CoA species or 2-trans- 4-trans-dienoyl-CoA species.<ref name=refname18 />  In comparing the products of the plant [[peroxisome]] and the multifunctional enzyme of rat [[liver]], the plant has no [[hydratase]] activity.<ref name=refname18 /> The Plant form did not form a 2-cis-isomer (from enoyl-CoA hydratase) or D- or L- 3 hydroxy derivative (L-(−)-3-hydroxyacyl-CoA dehydrogenase): products of multifunctional enzyme of rat [[liver]].<ref name=refname18 /> The turnover rates of these the two sub divisions of [[peroxisome]]s are very different. The Kcat/Km ratio in [[cotyledon]]s is 10^6 M-1s-1 which outperforms the ratio .07 * 10^6 M-1s-1.<ref name=refname18 /> Due to a high turnover rate, the plant [[peroxisome]]s contain a lesser amount of enoyl-CoA isomerase than their counterparts in the rat [[liver]].<ref name=refname18 />

In rat liver, [[mitochondria]]l enoyl CoA isomerase and peroxisomal enoyl CoA isomerase embedded in the multifunctional enzyme have similarities in the primary structure sequence.<ref name=refname19 /> When comparing the amino-terminal half of [[E. coli]] against the amino-terminal half of rat [[liver]], there were primary and secondary structure similarities towards the middle of the amino-terminal end.<ref name=refname19 /> This conserved region must be important for structure and function of this specific enzyme since showing equally in both [[E. coli]] and rat [[liver]].<ref name=refname19 /><ref name=refname24 />

==Enzyme structure==
All classes of enoyl-CoA [[isomerase]]s belong to a family of [[enzyme]]s, the [[hydratase]]/[[isomerase]] or [[crotonase]] superfamily, and when examined with [[x-ray crystallography]], exhibit a common structural feature of the family, the [[N-terminal]] core with a spiral fold composed of four turns, each turn consisting of two [[beta-sheet]]s and one [[alpha-helix]].<ref name="refname8" />

In enoyl-CoA [[isomerase]], the two [[beta-sheet]]s are part of the [[catalytic site]], since the NH groups of [[Amino acid|residues]] following the [[beta-sheet]]s attach to the [[carbonyl]] [[oxygen]] of the acyl-CoA [[Reaction intermediate|intermediate]]. The formation of this [[oxyanion hole]] stabilizes the [[transition state]] of the [[enzyme]]-catalyzed reaction.<ref name="refname4" />

[[File:Catalytic Site on Enoyl-CoA Isomerase in Yeast.png|thumb|Figure 2: Catalytic Sites of Enoyl-CoA Isomerase in Yeast]]

Moreover, a [[glutamate]] [[Amino acid|residue]] located next to [[body cavities]] filled with water molecules and lined with [[hydrophobic]] or [[apolar]] [[side chain]]s has also been identified as a part of the [[catalytic site]]. In its [[deprotonated]] form, the [[glutamate]] can act as a [[base (chemistry)|base]] and remove a [[proton]] from the acyl-CoA [[Reaction intermediate|intermediate]]. The [[body cavities]] aid in rearranging the [[glutamate]] [[side chain]] to retain the [[proton]] and later deliver it back to the acyl-CoA, on a different [[carbon]] position.<ref name="refname4" />

[[File:Trimer Disk of Enoyl-CoA Isomerase in Yeast.png|thumb|Figure 3: Trimer Disk of Enoyl-CoA Isomerase in Yeast]]

The NH-containing [[Amino acid|residues]] have been identified as Ala70 and Leu126 and the [[glutamate]] as Glu158 in [[peroxisomal]] [[enzyme]]s in a [[yeast]] species, ''[[Saccharomyces cerevisiae]]''. Their relative locations on the enzyme can be compared in Figure 2.<ref name="refname4" />

The [[enzyme]]s of the [[hydratase]]/[[isomerase]] or [[crotonase]] superfamily are typically [[trimer (chemistry)|trimer]]ic disks [[dimer (chemistry)|dimer]]ized into [[hexamer]]s. The wide range of their [[substrate (biochemistry)|substrate]]-[[enzyme]] specificity derives from the variations in the distances between the [[trimer (chemistry)|trimer]]ic disks and their orientation.<ref name="refname9" /> However, the [[human]] [[mitochondrial]] enoyl-CoA [[isomerase]] is a [[trimer (chemistry)|trimer]] and orients the [[fatty acid]] tail in a completely different direction from that seen in the [[hexamers]].<ref name="refname6" /> The [[trimer (chemistry)|trimer]]ic disk of [[peroxisomal]] [[enzymes]] in ''[[Saccharomyces cerevisiae]]'' is displayed in Figure 3.<ref name="refname9" />

==Enzyme history==
Enoyl-CoA [[isomerase]] was first identified and purified from [[rat]] [[liver]] [[mitochondria]] in the 1960s and 1970s via [[gel filtration]] and [[ion exchange chromatography]].<ref name="refname10" /> Since then, all classes of enoyl-CoA [[isomerase]], [[mitochondrial]], [[peroxisomal]] and multifunctional, have been identified in different organisms, including more [[mammal]]s, [[plant]]s, and [[unicellular]] organisms.

By 1994, using the [[rat]] enoyl-CoA [[isomerase]] [[cDNA]] as a [[hybridization probe]], [[human]] enoyl-CoA [[isomerase]] [[cDNA]] could be [[sequenced]] and [[cloned]].<ref name="refname2" /> In the same year, the protein itself was isolated, not by [[Chemistry|affinity]] to [[rat]] [[antibody]] or [[cDNA]] [[Atom probe|probe]]s,<ref name="refname3" /> but by co[[List of purification methods in chemistry|purification]] with a [[transferase]], human glutathione S-transferases.<ref name="refname11" />

In the attempts to examine the [[human]] enoyl-CoA [[isomerase]] in detail, the [[mitochondrial]] [[enzyme]] in the [[mammalian]] liver was identified as a potential [[biological marker]] for [[metabolic disease]]s due to its elevated levels in defective [[cell (biology)|cell]]s, and linked defects in [[fatty acid]] [[beta-oxidation]] to [[human]] diseases,<ref name="refname11" /> to be specified in the next section.

==Medical relevance==
In [[human]]s, defects in the [[beta-oxidation]] mechanism result in hypoketotic [[hyperglycemia]], a [[symptom]] of [[starvation]], due to the inefficient utilization of [[fatty acid]]s as a primary source of [[energy]].<ref name="refname7"/> The [[metabolic disease]] was found to be on a [[genetics|genetic]] level: [[rat]]s without the [[gene]]s for enoyl-CoA [[isomerase]] also displayed high [[blood glucose level]]. Moreover, a [[biological marker]] for this condition may have been identified as the [[urine]] of these [[rat]]s included high concentrations of medium chain [[Saturation (chemistry)|unsaturated]] [[dicarboxylic acids]], a condition called dicarboxylic aciduria.<ref name="refname7"/>

More recent studies link [[hepatitis C virus]] (HCV) infection to defects in [[fatty acid degradation]], specifically, to that in enoyl-CoA [[isomerase]].<ref name="refname12"/> [[Hepatitis C virus|HCV]] is the leading cause of [[chronic hepatitis]], [[cirrhosis]], and [[liver cancer]], and more than 180 million people are affected globally.<ref name="refname13"/> Due to the prolonged [[latency period|latency]] of the [[virus]] and no existing cures to rid the [[virus]] specifically,<ref name="refname14"/> [[Hepatitis C virus|HCV]] is a serious problem that is causing more deaths than [[HIV/AIDS]] in the [[United States]],<ref name="refname15"/> but its threat still do not receive adequate attention. The need for a [[Hepatitis C virus|HCV]]-specific treatment is essential, and according to John Ward, the director of the [[Centers for Disease Control and Prevention|CDC]] Hepatitis Division, it can save up to 120,000 lives.<ref name="refname15"/>

According to [[protein]] profiling in the [[human]] [[liver]] [[biopsies]] of [[Hepatitis C virus|HCV]] patients, a correlation was initially discovered between dysfunctional [[mitochondrial]] processes, which include [[beta-oxidation]], and [[Hepatitis C virus|HCV]].<ref name="refname16"/> As a matter of fact, [[lipid]]s play an important role in the [[DNA replication|replication]] cycle of [[Hepatitis C virus|HCV]], and in the "[[in vivo]]" samples from [[Hepatitis C virus|HCV]] patients, many [[lipid]]s were found in abundance to aid [[Hepatitis C virus|HCV]] in [[virus]] uptake, [[RNA replication]], and secretion from [[host cell]]s. [[Enzyme]]s that regulate [[fatty acid metabolism]], including enoyl-CoA [[isomerase]], were also similarly [[upregulated]].<ref name="refname12"/> [[Gene silencing]] techniques revealed that enoyl-CoA [[isomerase]] is essential in [[Hepatitis C virus|HCV]] [[RNA replication]], and opened ways to stop [[Hepatitis C virus|HCV]] infection on an [[intracellular]] level.<ref name="refname12"/>

==See also==
* [[Fatty acid metabolism]]
* [[Isomerase]]
* [[2,4-dienoyl-CoA reductase 1]]

==References==
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<ref name="refname4">{{cite journal |vauthors=Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK |title=The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase |journal=J. Mol. Biol. |volume=309 |issue=4 |pages=845–53 |date=June 2001 |pmid=11399063 |doi=10.1006/jmbi.2001.4671 |url=http://linkinghub.elsevier.com/retrieve/pii/S0022-2836(01)94671-6}}</ref>

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<ref name="refname7">{{cite journal |vauthors=Janssen U, Stoffel W |title=Disruption of mitochondrial beta -oxidation of unsaturated fatty acids in the 3,2-trans-enoyl-CoA isomerase-deficient mouse |journal=J. Biol. Chem. |volume=277 |issue=22 |pages=19579–84 |date=May 2002 |pmid=11916962 |doi=10.1074/jbc.M110993200 |url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=11916962}}</ref>

<ref name="refname8">{{cite journal |vauthors=Gurvitz A, Mursula AM, Firzinger A |title=Peroxisomal Delta3-cis-Delta2-trans-enoyl-CoA isomerase encoded by ECI1 is required for growth of the yeast Saccharomyces cerevisiae on unsaturated fatty acids |journal=J. Biol. Chem. |volume=273 |issue=47 |pages=31366–74 |date=November 1998 |pmid=9813046 |doi= 10.1074/jbc.273.47.31366|url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=9813046|display-authors=etal}}</ref>

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<ref name="refname11">{{cite journal |vauthors=Takahashi Y, Hirata Y, Burstein Y, Listowsky I |title=Delta 3, delta 2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferases from S-hexylglutathione affinity matrices |journal=Biochem. J. |volume=304 |issue= 3|pages=849–52 |date=December 1994 |pmid=7818490 |pmc=1137411 |doi= |url=}}</ref>

<ref name="refname12">{{cite journal |vauthors=Rasmussen AL, Diamond DL, McDermott JE |title=Systems virology identifies a mitochondrial fatty acid oxidation enzyme, dodecenoyl coenzyme A delta isomerase, required for hepatitis C virus replication and likely pathogenesis |journal=J. Virol. |volume=85 |issue=22 |pages=11646–54 |date=November 2011 |pmid=21917952 |doi=10.1128/JVI.05605-11 |url=http://jvi.asm.org/cgi/pmidlookup?view=long&pmid=21917952 |pmc=3209311|display-authors=etal}}
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<ref name="refname15">{{cite news |title=Hepatitis C Kills More Americans Than HIV/AIDS |url=http://www.voanews.com/english/news/health/Hepatitis-C-Kills-More-Americans-Than-HIVAIDS-140572713.html |newspaper=Voice of America, Health |date=27 February 2012 |accessdate=3 March 2012}}</ref>

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<ref name="refname24">{{cite journal |authors=Aner Gurvitz, Anu M. Mursula, Andreas Firzinger, Barbara Hamilton, Seppo H. Kilpela ̈ inen, Andreas Hartig, Helmut Ruis, J. Kalervo Hiltunen, and Hanspeter Rottensteiner |title=Peroxisomal delta3-cis-delta2-trans-Enoyl-CoA Isomerase Encoded by ECI1 Is Required for Growth of the Yeast Saccharomyces cerevisiae on Unsaturated Fatty Acids |journal=Biological Chemistry |volume=273 |pages=31366–31374 |year=1998 |url=http://www.jbc.org/content/273/47/31366.full.pdf |issue=47 |doi=10.1074/jbc.273.47.31366 |pmid=9813046}}</ref>

<ref name="refname25">{{cite journal |authors=Anu M. Mursula, Daan M. F. van Aalten, J. Kalervo Hiltunen and Rik K. Wierenga |title=The Crystal Structure of delta3-delta2-Enoyl-CoA Isomerase |journal=Molecular Biology |volume=309 |pages=845–853 |year=2001 |url=http://www.sciencedirect.com/science/article/pii/S0022283601946716# |doi=10.1006/jmbi.2001.4671 |pmid=11399063 |issue=4}}</ref>

<ref name="refname26">{{cite journal |author1=Gerhard Muller-Newen |author2=Uwe Janssen |author3=Wilhelm Stoffel |title=Enoyl-CoA hydratase and isomerase form a superfamily with a common active site glutamate residue |journal=Eur. J. Biochem. |volume=228 |pages=68–73 |year=1995 |url=http://onlinelibrary.wiley.com/store/10.1111/j.1432-1033.1995.0068o.x/asset/j.1432-1033.1995.0068o.x.pdf?v=1&t=hdxsifc3&s=0e59efe749648b0785362abd8ff8ad849471c1e2 |doi=10.1111/j.1432-1033.1995.tb20230.x}}</ref>

<ref name="refname27">{{cite journal |author1=Dongyan Zhang |author2=Wenfeng Yu |author3=Brian V. Geisbrecht |author4=Stephen J. Gould |author5=Howard Sprecher |author6=Horst Schulz |title=Functional Characterization of delta3,delta2-Enoyl-CoA Isomerases from Rat Liver |journal=Biological Chemistry |volume=277 |pages=9127–9132 |year=2002 |url=http://www.jbc.org/content/277/11/9127.full.pdf |issue=11 |doi=10.1074/jbc.m112228200}}</ref>

}}

{{Lipid metabolism enzymes}}
{{Intramolecular oxidoreductases}}
{{Enzymes}}
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{{Use dmy dates|date=April 2017}}

[[Category:EC 5.3.3]]