| 5-phosphonooxy-L-lysine phospho-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.134 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
5-Phosphonooxy-L-lysine phospho-lyase (EC 4.2.3.134, 5-phosphohydroxy-L-lysine ammoniophospholyase, AGXT2L2 (gene)) is an enzyme with systematic name (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming). [1] [2] This enzyme catalyses the following chemical reaction
- (5R)-5-phosphonooxy-L-lysine + H2O (S)-2-amino-6-oxohexanoate + NH3 + phosphate
This enzyme is a pyridoxal-phosphate protein.
- ^ Tsai CH, Henderson LM (September 1974). "Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase". The Journal of Biological Chemistry. 249 (18): 5784–9. doi: 10.1016/S0021-9258(20)79885-6. PMID 4412716.
- ^ Veiga-da-Cunha M, Hadi F, Balligand T, Stroobant V, Van Schaftingen E (March 2012). "Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine". The Journal of Biological Chemistry. 287 (10): 7246–55. doi: 10.1074/jbc.m111.323485. PMC 3293546. PMID 22241472.
- 5-phosphonooxy-L-lysine+phospho-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| 5-phosphonooxy-L-lysine phospho-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.2.3.134 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
5-Phosphonooxy-L-lysine phospho-lyase (EC 4.2.3.134, 5-phosphohydroxy-L-lysine ammoniophospholyase, AGXT2L2 (gene)) is an enzyme with systematic name (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming). [1] [2] This enzyme catalyses the following chemical reaction
- (5R)-5-phosphonooxy-L-lysine + H2O (S)-2-amino-6-oxohexanoate + NH3 + phosphate
This enzyme is a pyridoxal-phosphate protein.
- ^ Tsai CH, Henderson LM (September 1974). "Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase". The Journal of Biological Chemistry. 249 (18): 5784–9. doi: 10.1016/S0021-9258(20)79885-6. PMID 4412716.
- ^ Veiga-da-Cunha M, Hadi F, Balligand T, Stroobant V, Van Schaftingen E (March 2012). "Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine". The Journal of Biological Chemistry. 287 (10): 7246–55. doi: 10.1074/jbc.m111.323485. PMC 3293546. PMID 22241472.
- 5-phosphonooxy-L-lysine+phospho-lyase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)