PMID:12596860: Difference between revisions
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!align=left |Citation | |||
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'''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 | |||
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!align=left |Abstract | |||
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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. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12596860 PubMed] | |||
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| | !align=left |Keywords | ||
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|- | Amino Acid Sequence; Ammonia-Lyases/chemistry; Ammonia-Lyases/genetics; Ammonia-Lyases/isolation & purification; Ammonia-Lyases/metabolism; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Amino Acid; beta-Alanine/analogs & derivatives; beta-Alanine/metabolism | ||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:19, 15 September 2013
| Citation |
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 | |
| Keywords |
Amino Acid Sequence; Ammonia-Lyases/chemistry; Ammonia-Lyases/genetics; Ammonia-Lyases/isolation & purification; Ammonia-Lyases/metabolism; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Amino Acid; beta-Alanine/analogs & derivatives; beta-Alanine/metabolism |
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