Search results for EHHADH

Showing 4 results out of 4

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Species

Types

Compartments

Reaction types

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Protein (2 results from a total of 2)

Identifier: R-HSA-400155
Species: Homo sapiens
Compartment: peroxisomal matrix
Primary external reference: UniProt: EHHADH: Q08426
Identifier: R-HSA-9033147
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: EHHADH: Q08426

Reaction (2 results from a total of 2)

Identifier: R-HSA-6809264
Species: Homo sapiens
Compartment: peroxisomal matrix
Peroxisomal EHHADH catalyzes the reaction of 3-hydroxyhexacosanoyl-CoA and NAD+ to form 3-ketohexacosanoyl-CoA and NADH + H+. The enzyme is bifunctional - an aminoterminal domain catalyzes the dehydrogenation of a variety of 3-hydroxyacyl-CoA's, the reaction annotated here, and a carboxyterminal domain catalyzes the hydration of a variety of trans-2,3-dehydroacyl-CoA's. 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).
Identifier: R-HSA-6809263
Species: Homo sapiens
Compartment: peroxisomal matrix
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).
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