Linked Life Data

8215365

Source:http://linkedlifedata.com/resource/pubmed/id/8215365

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pubmed-article:8215365pubmed:abstractTextThe lysA gene of Bacillus methanolicus MGA3 was cloned by complementation of an auxotrophic Escherichia coli lysA22 mutant with a genomic library of B. methanolicus MGA3 chromosomal DNA. Subcloning localized the B. methanolicus MGA3 lysA gene into a 2.3-kb SmaI-SstI fragment. Sequence analysis of the 2.3-kb fragment indicated an open reading frame encoding a protein of 48,223 Da, which was similar to the meso-diaminopimelate (DAP) decarboxylase amino acid sequences of Bacillus subtilis (62%) and Corynebacterium glutamicum (40%). Amino acid sequence analysis indicated several regions of conservation among bacterial DAP decarboxylases, eukaryotic ornithine decarboxylases, and arginine decarboxylases, suggesting a common structural arrangement for positioning of substrate and the cofactor pyridoxal 5'-phosphate. The B. methanolicus MGA3 DAP decarboxylase was shown to be a dimer (M(r) 86,000) with a subunit molecular mass of approximately 50,000 Da. This decarboxylase is inhibited by lysine (Ki = 0.93 mM) with a Km of 0.8 mM for DAP. The inhibition pattern suggests that the activity of this enzyme in lysine-overproducing strains of B. methanolicus MGA3 may limit lysine synthesis.lld:pubmed
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pubmed-article:8215365pubmed:articleTitleCloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes.lld:pubmed
pubmed-article:8215365pubmed:affiliationDepartment of Biochemistry, University of Minnesota, St. Paul 55108.lld:pubmed
pubmed-article:8215365pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8215365pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:8215365pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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