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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

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

trans-2,3-dehydropristanoyl-CoA + H2O → 3-hydroxypristanoyl-CoA

Reactome: R-HSA-389986
Compartment: peroxisomal matrix
Rhea: None recorded

Inputs

trans-2,3-dehydropristanoyl-CoACHEBI:77293, C40H66N7O17P3S, peroxisomal matrix
H2OCHEBI:15377, H2O, peroxisomal matrix

Outputs

3-hydroxypristanoyl-CoACHEBI:63914, C40H72N7O18P3S, peroxisomal matrix

Catalysed by

3-hydroxyacyl-CoA dehydratase activity of HSD17B4 dimer [peroxisomal matrix]EC 4.2.1.150

Literature

Mutational spectrum of D-bifunctional protein deficiency and structure-based genotype-phenotype analysis Am J Hum Genet, 2006
Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase J Biochem (Tokyo), 1996
Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein J Biochem, 1997
Identification of the peroxisomal beta-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids J. Lipid Res., 2004