Lakshman, Meena ; Shenoy, B. C. ; Raghavendra Rao, M. R. (1981) Purification and properties of diaminopimelate decarboxylase of Micrococcus glutamicus Journal of Biosciences, 3 (2). pp. 89-104. ISSN 0250-5991
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Official URL: http://www.ias.ac.in/jarch/jbiosci/3/89-104.pdf
Related URL: http://dx.doi.org/10.1007/BF02702651
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 formeso diaminopimelate was 0.5 mM and that for pyridoxal-5'-phosphate was 0.6 μM. 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 |
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Source: | Copyright of this article belongs to Indian Academy of Sciences. |
Keywords: | Micrococcus Glutamicus; Diaminopimelate Decarboxylase; Pyridoxal Phosphate; Meso-diaminopimelate |
ID Code: | 33278 |
Deposited On: | 30 Mar 2011 13:17 |
Last Modified: | 17 May 2016 16:07 |
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