Methionine Regeneration and Aminotransferases in Bacillus Subtilis, Bacillus Cereus, and Bacillus Anthracis

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Authors
  1. Berger, B.J.
  2. English, S.
  3. Chan, G
  4. Knodel, M.H.
Corporate Authors
Defence R&D Canada - Suffield, Ralston ALTA (CAN)
Abstract
The conversion of ketomethiobutyrate in methionine has been previously examined in a number of organisms, wherein the aminotrasferases responsible for the reaction have been found to be members of the Ia subfamily. The genome of Bacillus subtilis has been found to contain no subfamily Ia aminotransferase sequences. Instead, the analogous enzymes in B. subtilis were found to be members of the If subfamily. These putative aspartate aminotransferases, the yugH, ywfG, ykrV, aspB, and patA gene products, have been cloned, expressed, and characterized for methionine regeneration activity. Only YkrV was able to convert ketomethiobutyrate to methionine, and it catalyzed the reaction only when glutamine was used as amino donor. In contrast, subcellular homogenates of B, subtilis and Bacillus cereus utilized leucine, isoleucine, valine, alanine, phenylalanine, and tyrosine as effective amino donors. The two putative brnached-chain aminotransferase genes in B. subtilis, ybgE and ywaA, were also cloned, expressed, and characterized. Both gene products effectively transaminiated branched-chain amino acids and ketoglutarate, but only YhgE converted ketomethinbutyrate to methionine. TRUNCATED
Keywords
Aminotransferases;Methionine recycling
Report Number
DRDC-SUFFIELD-SL-2002-141 — Scientific Literature
Date of publication
27 Jan 2003
Number of Pages
15
Reprinted from
Journal of Bacteriology, 2003, p 2418-2431
DSTKIM No
CA022347
CANDIS No
519276
Format(s):
Hardcopy

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