CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.90 | Alpha-Beta Complex |
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3.90.226 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
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3.90.226.10 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Domain Context
CATH Clusters
Superfamily | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Functional Family | Fatty acid oxidation complex subunit alpha |
Enzyme Information
4.2.1.17 |
Enoyl-CoA hydratase.
based on mapping to UniProt P28793
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).
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1.1.1.35 |
3-hydroxyacyl-CoA dehydrogenase.
based on mapping to UniProt P28793
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
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5.1.2.3 |
3-hydroxybutyryl-CoA epimerase.
based on mapping to UniProt P28793
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
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5.3.3.8 |
Delta(3)-Delta(2)-enoyl-CoA isomerase.
based on mapping to UniProt P28793
(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.
-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
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UniProtKB Entries (1)
P28790 |
FADA_PSEFR
Pseudomonas fragi
3-ketoacyl-CoA thiolase
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PDB Structure
PDB | 1WDM |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex
Embo J.
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