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    • Keywords


      Micrococcus glutamicus ; diaminopimelate decarboxylase; pyridoxal phosphate; meso-diaminopimelate

    • Abstract


      Diaminopimelate decarboxylase (EC ofMicrococcus glutamicus ATCC 13059 was purified to homogeneity. The enzyme had an apparent molecular weight of 191,000 as determined by gel filtration on Sephadex G-200. At protein concentrations of 20 and 10 μg per ml and in the absence of pyridoxal-5′-phosphate, it dissociated into a species of molecular weight 94,000. The polypeptide chain molecular weight as determined by sodium dodecyl sulphate Polyacrylamide gel electrophoresis was 100,000. TheKm formeso diaminopimelate was 0.5 mM and that for pyridoxal-5′-phosphate was 0.6 μI. Sulphydryl groups and pyridoxal-5′-phosphate were essential for activity and stability. The enzyme was inhibited significantly by L-lysine and DL-aspartic β-semialdehyde.

    • Author Affiliations


      Meena Lakshman1 B C Shenoy1 M R Raghavendra Rao1

      1. Discipline of Biochemistry and Applied Nutrition, Central Food Technological Research Institute, Mysore - 570 013
    • Dates

  • Journal of Biosciences | News

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