| EC |
4.3.1.15 |
| Accepted name: |
diaminopropionate ammonia-lyase |
| Reaction: |
2,3-diaminopropanoate + H2O = pyruvate + 2 NH3 |
| Other name(s): |
diaminopropionatase; α,β-diaminopropionate ammonia-lyase; 2,3-diaminopropionate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase; 2,3-diaminopropanoate ammonia-lyase (adding H2O; pyruvate-forming) |
| Systematic name: |
2,3-diaminopropanoate ammonia-lyase (adding water; pyruvate-forming) |
| Comments: |
A pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 51901-19-0 |
| References: |
| 1. |
Nagasawa, T., Tanizawa, K., Satoda, T., Yamada, H. Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5′-phosphate binding peptide. J. Biol. Chem. 263 (1988) 958–964. [PMID: 3275662] |
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| [EC 4.3.1.15 created 1999] |
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