Characterization of Potential Antimicrobial Targets in Bacillus spp. II. Branched-chain Aminotransferase and Methionine Regeneration in B. Cereus and B. Anthracis

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Authors
  1. Berger, B.J.
  2. English, S.
  3. Knodel, M.H.
  4. Chan, G.
Corporate Authors
Defence R&D Canada - Suffield, Ralston ALTA (CAN);Canada West Biosciences, Calgary ALTA (CAN)
Abstract
The final step of methionine recycling from methylthioadenosine has been examined in the gram-positive bacteria Bacillus cereus and B. anthracis. Subcellular homogenates were able to convert ketomethiobutyrate to methionine using leucine, isoleucine, valine, phenylalanine, tyrosine, tryptophan, and alanine as amino donors. Four putative family III aminotransferases, two with homology to branched-chain amino acid aminotransferases and two with homology to D-amino acid aminotransferases, were cloned form B. cereus. The two branched-chain aminotransferases were found to have a low sequence identity with the corresponding enzymes from B. subtilis, indicative of membership of a different subamily. After expression of the B. cereus enzymes in Escherichia coli and subsequent purification, one branched chain aminotransferase, designated Bc-BCAT2, was found to catalyse methionine regeneration using leucine, isoleucine, valine, phenylalanine, tryosine, and tryprophan as amino donors. The homogue of BC-BCAT2 was cloned from B. anthracis and designated Ba-BCAT2. TRUNCATED

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Keywords
Biological Warfare Agents;Antibiotic sensitivity;Methionine recycling;Aminotransferases;Inhibition;Canaline
Report Number
DRDC-SUFFIELD-TR-2002-094 — Technical Report
Date of publication
01 Sep 2002
Number of Pages
41
DSTKIM No
CA021493
CANDIS No
518214
Format(s):
Hardcopy;Document Image stored on Optical Disk

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