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B6db activities: 4.3.1.15

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
 

Family 

4.3.1.15 (0)
 
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
 
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.

Articles on 4.3.1.15
 
last changed 2019/06/20 13:24

B6db activities