CATH Classification
Domain Context
CATH Clusters
| Superfamily | N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2 |
| Functional Family | Peroxisomal bifunctional enzyme |
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).
|
| 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).
|
| 5.3.3.8 |
Dodecenoyl-CoA isomerase.
based on mapping to UniProt P07896
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
-!- Also catalyzes the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C(6) to C(12).
|
UniProtKB Entries (1)
| P07896 |
ECHP_RAT
Rattus norvegicus
Peroxisomal bifunctional enzyme
|
PDB Structure
| PDB | 1ZCJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural Studies of MFE-1: the 1.9A Crystal Structure of the Dehydrogenase Part of Rat Peroxisomal MFE-1
J.Mol.Biol.
|