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Literature summary for 5.1.1.3 extracted from

  • Sengupta, S.; Ghosh, S.; Nagaraja, V.
    Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme (2008), Microbiology, 154, 2796-2803.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
C185S decrease in racemization activity, mutant retains its gyrase inhibition ability Mycobacterium tuberculosis
C75S decrease in racemization activity, mutant retains its gyrase inhibition ability Mycobacterium tuberculosis
C75SC185S less than 10% of wild-type activity, mutant retains its gyrase inhibition ability Mycobacterium tuberculosis
additional information overexpression in vivo provides resistance to the action of ciprofloxacin Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mycobacterium tuberculosis enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity ?
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?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity Mycobacterium tuberculosis ?
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?