B6db families : 4_3_1

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4.3.1.15

Activity

4.3.1.15

Description

Diaminopropionate ammonia-lyase

PDB

4D9I;5YGR;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type II

Number of sequences

Sequences in seed alignment

Bacteria

CAG20396 (Photobacterium profundum); ZP_00046727 (Lactobacillus gasseri); DPAL_ECOLI (Escherichia coli); AAO34726 (Clostridium tetani); DPAL_SALTY (Salmonella typhimurium); ZP_00098586 (Desulfitobacterium hafniense); AAO82290 (Enterococcus faecalis);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

DPAL_ECOLI

Domain interval

38-377

Catalytic site

77 K

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