| EC |
4.2.3.134 |
| Accepted name: |
5-phosphooxy-L-lysine phospho-lyase |
| Reaction: |
(5R)-5-phosphooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH3 + phosphate |
| Other name(s): |
5-phosphohydroxy-L-lysine ammoniophospholyase; AGXT2L2 (gene name); (5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming); 5-phosphonooxy-L-lysine phospho-lyase |
| Systematic name: |
(5R)-5-phosphooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming) |
| Comments: |
A pyridoxal-phosphate protein. Has no activity with phosphoethanolamine (cf. EC 4.2.3.2, ethanolamine-phosphate phospho-lyase). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Tsai, C.H. and Henderson, L.M. Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase. J. Biol. Chem. 249 (1974) 5784–5789. [PMID: 4412716] |
| 2. |
Veiga-da-Cunha, M., Hadi, F., Balligand, T., Stroobant, V. and Van Schaftingen, E. Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J. Biol. Chem. 287 (2012) 7246–7255. [DOI] [PMID: 22241472] |
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| [EC 4.2.3.134 created 2012] |
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