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4.3.1.15 |
| Description |
Diaminopropionate ammonia-lyase |
| Alternative names |
Diaminopropionatase;
Alpha,beta-diaminopropionate ammonia-lyase. |
| Catalyzed reaction |
2,3-diaminopropionate = pyruvate + 2 NH(3). |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- Active towards both D- and L-diaminopropionate.
-!- D- and L-Serine are poor substrates. |
| PDB |
4D9I; 5YGR; |
| Organisms |
-Eubacteria |
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| Links |
Enzyme (activities) 4.3.1.15
BRENDA (activities) 4.3.1.15
KEGG (pathways) 4.3.1.15
PLPMDB (PLP mutants) 4.3.1.15
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| References |
Deka G, Bisht S, Savithri HS, Murthy MRN (2018) Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features J Struct Biol 202 118-128. Bisht S, Rajaram V, Bharath SR, Kalyani JN, Khan F, Rao AN, Savithri HS, Murthy MR (2012) Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis J Biol Chem 287 20369-81. Khan, F.; Jala, V.R.; Rao, N.A.; Savithri, H.S. (2003) Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella typhimurium Biochem Biophys Res Commun 306 1083-8. Uo, T.; Yoshimura, T.; Nishiyama, T.; Esaki, N. (2002) Gene cloning, purification, and characterization of 2,3-diaminopropionate ammonia-lyase from Escherichia coli Biosci Biotechnol Biochem 66 2639-44. Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H. (1988) 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 263 958-64. |
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| last changed |
2019/06/20 13:24 |
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