Propanoyl-CoA acyltransferase
Propanoyl-CoA acyltransferase | ||
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Properties of human protein | ||
Mass / length primary structure | 547 amino acids | |
Isoforms | SCPx, SCP2 | |
Identifier | ||
Gene name | SCP2 | |
External IDs | ||
Enzyme classification | ||
EC, category | 2.3.1.176 , transferase | |
Response type | Transfer of a propanoic acid residue | |
Substrate | 3α, 7α, 12α-trihydroxy-5β-24-oxo-cholestanoyl-CoA + CoA-SH | |
Products | Choloyl-CoA + propanoyl-CoA | |
Occurrence | ||
Parent taxon | Animals, mushrooms |
Propanoyl-CoA acyltransferase (also: sterol carrier protein (SCP) , non-specific lipid-transfer protein ) is the enzyme in animals and fungi, that the biosynthesis of choloyl-CoA, a precursor of the cholic acid (a bile acid ) catalyzed . It is localized in the cytosol and mitochondria of the peroxisomes . It binds to PEX5 for peroxisome import . In humans, SCP is mainly produced in the liver , fibroblasts and placenta . In Zellweger's syndrome , the SCP activity is reduced due to the lack of peroxisomes.
Catalyzed reaction
Propanoic acid is transferred from 3α, 7α, 12α-trihydroxy-5β-24-oxo-cholestanoyl-CoA to CoA-SH, choloyl-CoA and propanoyl-CoA are formed.
Individual evidence
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Bile Acid Metabolism - Learning and Teaching Materials