| L-serine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Serine dehydratase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 4.3.1.17 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
- L-serine = pyruvate + NH3 (overall reaction)
- (1a) L-serine = 2-aminoprop-2-enoate + H2O
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
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 ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P5J, 1PWE, 1PWH, and 2IQQ.
References
- Ramos F, Wiame JM (1982). "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123 (3): 571–6. doi: 10.1111/j.1432-1033.1982.tb06570.x. PMID 7042346.
- Simon D, Hoshino J, Kroger H (1973). "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta. 321 (1): 361–8. doi: 10.1016/0005-2744(73)90091-0. PMID 4750769.
- Suda M, Nakagawa H (1971). L-Serine dehydratase (rat liver). Methods Enzymol. Vol. 17B. pp. 346–351. doi: 10.1016/0076-6879(71)17060-7.
- Sagers RD, Carter JE (1971). L-Serine dehydratase (Clostridium acidiurica). Methods Enzymol. Vol. 17B. pp. 351–356. doi: 10.1016/0076-6879(71)17061-9.
- Robinson WG, Labow R (1971). L-Serine dehydratase (Escherichia coli). Methods Enzymol. Vol. 17B. pp. 356–360. doi: 10.1016/0076-6879(71)17062-0.
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
| L-serine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
Serine dehydratase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 4.3.1.17 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
- L-serine = pyruvate + NH3 (overall reaction)
- (1a) L-serine = 2-aminoprop-2-enoate + H2O
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
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 ammonia-lyase (pyruvate-forming). Other names in common use include serine deaminase, L-hydroxyaminoacid dehydratase, L-serine deaminase, L-serine dehydratase, and L-serine hydro-lyase (deaminating). This enzyme participates in glycine, serine, threonine and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1P5J, 1PWE, 1PWH, and 2IQQ.
References
- Ramos F, Wiame JM (1982). "Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae". Eur. J. Biochem. 123 (3): 571–6. doi: 10.1111/j.1432-1033.1982.tb06570.x. PMID 7042346.
- Simon D, Hoshino J, Kroger H (1973). "L-serine dehydratase from rat liver. Purification and some properties". Biochim. Biophys. Acta. 321 (1): 361–8. doi: 10.1016/0005-2744(73)90091-0. PMID 4750769.
- Suda M, Nakagawa H (1971). L-Serine dehydratase (rat liver). Methods Enzymol. Vol. 17B. pp. 346–351. doi: 10.1016/0076-6879(71)17060-7.
- Sagers RD, Carter JE (1971). L-Serine dehydratase (Clostridium acidiurica). Methods Enzymol. Vol. 17B. pp. 351–356. doi: 10.1016/0076-6879(71)17061-9.
- Robinson WG, Labow R (1971). L-Serine dehydratase (Escherichia coli). Methods Enzymol. Vol. 17B. pp. 356–360. doi: 10.1016/0076-6879(71)17062-0.
|
| This enzyme-related article is a stub. You can help Wikipedia by expanding it. |