CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.40 | 3-Layer(aba) Sandwich |
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3.40.50 | Rossmann fold |
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3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
Superfamily | NAD(P)-binding Rossmann-like Domain |
Functional Family | peroxisomal bifunctional enzyme isoform X1 |
Enzyme Information
1.1.1.35 |
3-hydroxyacyl-CoA dehydrogenase.
based on mapping to UniProt P07896
(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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4.2.1.17 |
Enoyl-CoA hydratase.
based on mapping to UniProt P07896
(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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5.3.3.8 |
Delta(3)-Delta(2)-enoyl-CoA isomerase.
based on mapping to UniProt P07896
(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)
P07896 |
ECHP_RAT
Rattus norvegicus
Peroxisomal bifunctional enzyme
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PDB Structure
PDB | 3ZW9 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
The Isomerase and Hydratase Reaction Mechanism of the Crotonase Active Site of the Multifunctional Enzyme (Type-1), as Deduced from Structures of Complexes with 3S-Hydroxy- Acyl-Coa.
FEBS J.
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