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Purification and properties of diaminopimelate decarboxylase of Micrococcus glutamicus
| Content Provider | CSIR - Central Food Technological Research Institute (CFTRI) |
|---|---|
| Author | Lakshman, Meena Shenoy, B. C. Rao, M. R. Raghavendra |
| Date of Submission | 1981-01-01 |
| 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 μgper 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. |
| Starting Page | 89 |
| Ending Page | 104 |
| Page Count | 16 |
| File Format | |
| Volume Number | 3 |
| Journal | Journal of Biosciences |
| Language | English |
| Access Restriction | Limited |
| Subject Keyword | Enzymes Meso Diaminopimelate Pyridoxal phosphate Wheat |
| Content Type | Text |
| Resource Type | Article |
