PM20D1 hydrolyzes oleoyl-phe

Stable Identifier
R-HSA-9673054
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Extracellular PM20D1 (N-fatty-acyl-amino acid synthase/hydrolase PM20D1) catalyzes the reversible hydrolysis of oleoyl-phe (N-(9Z-octadecenoyl)-L-phenylalanine) to form L-phenylalanine (L-phe) and oleate ((9Z)-octadecenoate). In addition to the hydrolysis of oleoyl-phe (N-(9Z-octadecenoyl)-L-phenylalanine) annotated here, purified PM20D1 can hydrolyze a variety of n-acyl amino acids (Long et al. 2016).

Literature References
PubMed ID Title Journal Year
27374330 The Secreted Enzyme PM20D1 Regulates Lipidated Amino Acid Uncouplers of Mitochondria

Long, JZ, Svensson, KJ, Bateman, LA, Lin, H, Kamenecka, T, Lokurkar, IA, Lou, J, Rao, RR, Chang, MR, Jedrychowski, MP, Paulo, JA, Gygi, SP, Griffin, PR, Nomura, DK, Spiegelman, BM

Cell 2016
Participants
Participant Of
Event Information
Catalyst Activity
Catalyst Activity
Title
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides of PM20D1 [extracellular region]
Physical Entity
Activity
Orthologous Events
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Created
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