O-phosphoserine sulfhydrylase
Class of enzymes / From Wikipedia, the free encyclopedia
In enzymology, an O-phosphoserine sulfhydrylase (EC 2.5.1.65) is an enzyme that catalyzes the chemical reaction
- O-phospho-L-serine + hydrogen sulfide L-cysteine + phosphate
Quick Facts Identifiers, EC no. ...
O-phosphoserine sulfhydrylase | |||||||||
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Identifiers | |||||||||
EC no. | 2.5.1.65 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Thus, the two substrates of this enzyme are O-phospho-L-serine and hydrogen sulfide, whereas its two products are L-cysteine and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O-phospho-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase. This enzyme is also called O-phosphoserine(thiol)-lyase. This enzyme participates in cysteine metabolism and sulfur metabolism.