In enzymology, an O-phosphoserine sulfhydrylase (EC 2.5.1.65) is an enzyme that catalyzes the chemical reaction
| O-phosphoserine sulfhydrylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
- O-phospho-L-serine + hydrogen sulfide L-cysteine + phosphate
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.
References
edit- Mino K, Ishikawa K (2003). "A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1". FEBS Lett. 551 (1–3): 133–8. doi:10.1016/S0014-5793(03)00913-X. PMID 12965218.
- Mino K, Ishikawa K (2003). "Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1". J. Bacteriol. 185 (7): 2277–84. doi:10.1128/JB.185.7.2277-2284.2003. PMC 151494. PMID 12644499.
- Mino K, Oda Y, Ataka M, Ishikawa K (2003). "Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1". Acta Crystallogr. D. 59 (Pt 2): 338–40. doi:10.1107/S0907444902017900. PMID 12554945.
