trans-2,3-dehydropristanoyl-CoA + H2O => 3-hydroxypristanoyl-CoA

Stable Identifier
Reaction [transition]
Homo sapiens
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Peroxisomal HSD17B4 dimer catalyzes the reaction of trans-2,3-dehydropristanoyl-CoA and H2O to form 3-hydroxypristanoyl-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 (Jiang et al. 1996, 1997). Defects in the enzyme are associated with a severe disorder of peroxisomal fatty acid metabolism in humans (Ferdinandusse et al. 2006).

Literature References
PubMed ID Title Journal Year
9089413 Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein

Souri, M, Hashimoto, T, Jiang, LL, Miyazawa, S

J Biochem 1997
16385454 Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis

Glumoff, T, Koski, MK, Oostheim, W, Wanders, RJA, Gloerich, J, Ylianttila, MS, Hiltunen, JK, Waterham, HR, Ferdinandusse, S

Am J Hum Genet 2006
8902629 Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase

Fukushima, H, Kobayashi, A, Matsuura, H, Hashimoto, T, Jiang, LL

J Biochem (Tokyo) 1996
Catalyst Activity

long-chain-enoyl-CoA hydratase activity of HSD17B4 dimer [peroxisomal matrix]

Orthologous Events
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