The enzyme Serine-sulfate ammonia-lyase (EC 4.3.1.10) catalyzes the chemical reaction
| serine-sulfate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.10 | ||||||||
| CAS no. | 9054-70-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- L-serine O-sulfate H2O pyruvate NH3 sulfate
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-serine-O-sulfate ammonia-lyase (pyruvate-forming). It is also called (L-SOS)lyase.
References
edit- Thomas JH, Tudball N (1967). "Studies on the enzymic degradation of L-serine O-sulphate by a rat liver preparation". Biochem. J. 105 (2): 467–72. doi:10.1042/bj1050467. PMC 1198333. PMID 5583990.467-72&rft.date=1967&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198333#id-name=PMC&rft_id=info:pmid/5583990&rft_id=info:doi/10.1042/bj1050467&rft.aulast=Thomas&rft.aufirst=JH&rft.au=Tudball, N&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1198333&rfr_id=info:sid/en.wikipedia.org:Serine-sulfate ammonia-lyase" class="Z3988">
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