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4.3.1.15 |
Activity |
4.3.1.15 |
Description |
Diaminopropionate ammonia-lyase |
PDB |
4D9I;5YGR; |
PLP Fold Type |
II |
PLP-dependent Domain |
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Number of sequences |
7 |
Sequences in seed alignment |
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Reference sequence |
DPAL_ECOLI |
Domain interval |
38-377 |
Catalytic site |
77 K |
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References |
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. Articles on 4.3.1.15 |
last changed |
2018/01/08 12:41 |
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