Purification and properties of diaminopimelate decarboxylase ofMicrococcus glutamicus
| Autor: | Meena Lakshman, B. C. Shenoy, M. R. Raghavendra Rao |
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| Rok vydání: | 1981 |
| Předmět: |
Micrococcus glutamicus
chemistry.chemical_classification Chromatography Sodium Size-exclusion chromatography chemistry.chemical_element General Medicine Diaminopimelate decarboxylase General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Enzyme chemistry Biochemistry Sephadex Pyridoxal phosphate General Agricultural and Biological Sciences Polyacrylamide gel electrophoresis |
| Zdroj: | Journal of Biosciences. 3:89-103 |
| ISSN: | 0973-7138 0250-5991 |
| DOI: | 10.1007/bf02702651 |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
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