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).
Chen, GL, Balfe, A, Erwa, W, Hoefler, G, Gaertner, J, Aikawa, J, Chen, WW
Lalwani, ND, Reddy, MK, Mangkornkanok-Mark, M, Reddy, JK
Ferdinandusse, S, Denis, S, van Roermund, CW, Wanders, RJ, Dacremont, G
Osumi, T, Hashimoto, T
Houten, SM, Denis, S, Argmann, CA, Jia, Y, Ferdinandusse, S, Reddy, JK, Wanders, RJ
3-hydroxyacyl-CoA dehydrogenase activity of EHHADH [peroxisomal matrix]
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