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| biopax3:comment |
|FRAME:CPLX-7855| is one of a small class of enzymes that use a covalently bound pyruvoyl prosthetic group. The pyruvoyl group is thought to act analogously to pyridoxal phosphate cofactor by forming a Schiff base with the amino group of the substrate and then serving as an electron sink to facilitate the decarboxylation |CITS: [2018773]|. Several of these enzymes, including |FRAME: CPLX-7792|, |FRAME: PHOSPHASERDECARB-CPLX|, |FRAME: CPLX0-2901|, and |FRAME: CPLX-6906|, are decarboxylases forming important biological amines. All of these enzymes are known to have the pyruvoyl prosthetic group attached via an amide linkage to the amino terminus of the α subunit. Pyruvoyl-containing enzymes are expressed as a zymogen which is processed post-translationally by a self-maturation cleavage called serinolysis. In this process the pyruvoul group is formed from a serine residue, splitting the presursor protein into two parts which become the α and β subunits. In some cases additional subunits may be involved. |FRAME:CPLX-7855| catalyzes the formation of |FRAME: L-1-PHOSPHATIDYL-ETHANOLAMINE| by decarboxylation of |FRAME: L-1-PHOSPHATIDYL-SERINE|. The human enzyme has not been purified. The gene was identified based on its similarity to genes from other organisms. The gene from Chinese hamster ovary cells has been verified biochemically to encode this activity by functional complementation |CITS: [2007589]|. The enzyme from rat liver has been purified |CITS:[1495416][8132055]|.
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| biopax3:dataSource | |
| biopax3:displayName |
phosphatidylserine decarboxylase
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| biopax3:standardName |
phosphatidylserine decarboxylase
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