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Purification and properties of diaminopimelate decarboxylase of Micrococcus glutamicus.

Meena, Lakshman. and Shenoy, B. C. and Raghavendra Rao, M. R. (1981) Purification and properties of diaminopimelate decarboxylase of Micrococcus glutamicus. Journal of Biosciences, 3 (2). pp. 89-104.

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Abstract

Diaminopimelate decarboxylase (EC 4.1.1.20) of Micrococcus 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. The Km for meso diaminopimelate was 0.5 mM and that for pyridoxal-5'-phosphate was 0.6 μΜ. 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.

Item Type: Article
Uncontrolled Keywords: Micrococcus glutamicus; diaminopimelate decarboxylase; pyridoxal phosphate; meso -diaminopimelate
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 21 Cereals > 04 Wheat
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 06 Mar 2018 04:32
Last Modified: 06 Mar 2018 04:32
URI: http://ir.cftri.com/id/eprint/5141

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