Reactome | EHHADH hydrates trans-2,3-dehydrohexacosanoyl-CoA

EHHADH hydrates trans-2,3-dehydrohexacosanoyl-CoA

Stable Identifier

R-HSA-6809263

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix

Synonyms

(2E)-hexacosenoyl-CoA + H2O => (3R)-hydroxyhexacosanoyl-CoA, trans-2,3-dehydrohexacosanoyl-CoA + H2O => 3-hydroxyhexacosanoyl-CoA (EHHADH)

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

EHHADH hydrates trans-2,3-dehydrohexacosanoyl-CoA

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Peroxisomal EHHADH catalyzes the reaction of trans-2,3-dehydrohexacosanoyl-CoA and H2O to form 3-hydroxyhexacosanoyl-CoA. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's, the reaction annotated here. The properties of the human enzyme are inferred from studies of its mouse and rat homologues and from enzymatic stdies of mutant yeast cells expressing the cloned human enzyme (Chen et al. 1991, Ferdinandusse et al. 2004; Houten et al. 2012; Lalwani et al. 1981; Osumi & Hashimoto 1979). The enzyme can also act on fatty dicarboxylic acids (not annotated here) (Houten et al, 2012).

Literature References

PubMed ID	Title	Journal	Year
6798973	Induction, immunochemical identity and immunofluorescence localization of an 80 000-molecular-weight peroxisome-proliferation-associated polypeptide (polypeptide PPA-80) and peroxisomal enoyl-CoA hydratase of mouse liver and renal cortex Mangkornkanok-Mark, M, Reddy, MK, Reddy, JK, Lalwani, ND	Biochem. J.	1981
1651711	Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro Chen, GL, Hoefler, G, Balfe, A, Erwa, W, Chen, WW, Aikawa, J, Gaertner, J	Biochem. Biophys. Res. Commun.	1991
15060085	Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids van Roermund, CW, Denis, S, Dacremont, G, Wanders, RJA, Ferdinandusse, S	J. Lipid Res.	2004
486181	Peroxisomal beta oxidation system of rat liver. Copurification of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase Osumi, T, Hashimoto, T	Biochem. Biophys. Res. Commun.	1979
22534643	Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids Jia, Y, Denis, S, Houten, SM, Wanders, RJA, Argmann, CA, Reddy, JK, Ferdinandusse, S	J. Lipid Res.	2012