PMID:12596860

Uo, T, Yoshimura, T, Nishiyama, T and Esaki, N (2002) Gene cloning, purification, and characterization of 2,3-diaminopropionate ammonia-lyase from Escherichia coli.Biosci. Biotechnol. Biochem. 66:2639-44

Abstract

2,3-Diaminopropionate ammonia-lyase (DAPAL), which catalyzes alpha,beta-elimination of 2,3-diaminopropionate regardless of its stereochemistry, was purified from Salmonella typhimurium. We cloned the Escherichia coli ygeX gene encoding a putative DAPAL and purified the gene product to homogeneity. The protein obtained contained pyridoxal 5'-phosphate and was composed of two identical subunits with a calculated molecular weight of 43,327. It catalyzed the alpha,beta-elimination of both D- and L-2,3-diaminopropionate. The results confirmed that ygeX encoded DAPAL. The enzyme acted on D-serine, but its catalytic efficiency was only 0.5% that with D-2,3-diaminopropionate. The enzymologic properties of E. coli DAPAL resembled those of Salmonella DAPAL, except that L-serine, D-and L-beta-Cl-alanine were inert as substrates of the enzyme from E. coli. DAPAL had significant sequence similarity with the catalytic domain of L-threonine dehydratase, which is a member of the fold-type II group of pyridoxal phosphate enzymes, together with D-serine dehydratase and mammalian serine racemase.

Links

PubMed

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
ygeX:Gene_Product(s)		GO:0008838	diaminopropionate ammonia-lyase activity	IDA: Inferred from Direct Assay		F	The authors cloned, expressed and purified YgeX and then assayed the purified protein for 2,3-Diaminopropionate ammonia-lyase activity (Table 1 & Figure 3).	complete
ygeX:Gene_Product(s)		GO:0019796	nonprotein amino acid catabolic process	ISA: Inferred from Sequence Alignment	UniProtKB:P40817	P	Similar to Salmonella typhimurium 2,3-Diaminopropionate ammonia-lyase, the YgeX gene product of E. coli appears to be involved in catalyzing alpha,beta-elimination of 2,3-diaminopropionate (Figure 1).	complete
edit table

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.