CATH Classification

Domain Context

CATH Clusters

Superfamily 2-enoyl-CoA Hydratase; Chain A, domain 1
Functional Family Peroxisomal bifunctional enzyme

Enzyme Information
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
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
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.

UniProtKB Entries (1)

Rattus norvegicus
Peroxisomal bifunctional enzyme

PDB Structure

External Links
Primary Citation
Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part.
Kasaragod, P., Midekessa, G.B., Sridhar, S., Schmitz, W., Kiema, T.R., Hiltunen, J.K., Wierenga, R.K.
FEBS Open Bio