3-hydroxypristanoyl-CoA + NAD+ => 3-ketoxypristanoyl-CoA + NADH + H+

Stable Identifier
R-HSA-389995
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Peroxisomal HSD17B4 dimer catalyzes the reaction of 3-hydroxypristanoyl-CoA and NAD+ to form 3-ketoxypristanoyl-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 (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
16385454 Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis

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

Am J Hum Genet 2006
9089413 Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein

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

J Biochem 1997
8902629 Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase

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

J Biochem (Tokyo) 1996
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
3-hydroxyacyl-CoA dehydrogenase activity of HSD17B4 dimer [peroxisomal matrix]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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