Purification and properties of diaminopimelate decarboxylase ofMicrococcus glutamicus |
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Authors: | Meena Lakshman B. C. Shenoy M. R. Raghavendra Rao |
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Affiliation: | (1) Discipline of Biochemistry and Applied Nutrition, Central Food Technological Research Institute, 570 013 Mysore |
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Abstract: | Diaminopimelate decarboxylase (EC 4.1.1.20) 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. TheK m 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. |
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Keywords: | Micrococcus glutamicus diaminopimelate decarboxylase pyridoxal phosphate meso-diaminopimelate |
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