Branched-Chain Amino Acid Aminotransferase and Methionine Formation in Mycobacterium Tuberculosis

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Authors
  1. Venos, E.S.
  2. Knodel, M.H.
  3. Radford, C.L.
  4. Berger, B.J.
Corporate Authors
Defence R&D Canada - Suffield, Ralston ALTA (CAN)
Abstract
Tuberculosis remains a major world-wide health threat which demands the discovery and characterization of new drug targets in order to develop future antimycobacterials. The regeneration of methionine consumed during polyamine biosynthesis is an important pathway present in many microorganisms. The final step of this pathway, the conversion of ketomethiobutyrate to methionine, can be performed by aspartate, typrosine, or branched-chain amino acid aminotransferases depending on the particular species examined. The gene coding for branched-chain amino acid aminotransferase in Mycobacterium tuberculosis H37Rv has been cloned, expressed, and characterized. The enzyme found to be a member of the aminotransferase IIIa subfamily, and closely related to the corresponding aminotransferase in Bacillus subtilis, but not to that found in B. anthracis or B. cereus. The amino donor preference for the formation of methionine from ketomethiobutyrate was for isoleucine, leucine, valine, glutamate, and phenylalanine. TRUNCATED
Report Number
DRDC-SUFFIELD-SL-2004-106 — Scientific Litearture
Date of publication
07 Oct 2004
Number of Pages
15
DSTKIM No
CA025053
CANDIS No
522587
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