Purification and properties of a homodimeric protocatechuate 4,5-dioxygenase from Rhizobium leguminosarum |
| |
Authors: | Yung Pin Chen Charles R Lovell |
| |
Institution: | (1) Department of Biological Sciences, University of South Carolina, 29208 Columbia, SC, USA |
| |
Abstract: | Protocatechuate 4,5-dioxygenase has been purified 100-fold from 4-hydroxybenzoate grown cells of Rhizobium leguminosarum biovar viceae. The purification yielded a homogeneous preparation with specific activity of 321 Units · mg-1 protein. The molecular weight of the homodimeric native protein was 120,000, with subunit molecular weight of 62,000. The optimum pH for catalytic activity was 9.5 and the K
m for protocatechuate was 20 M. Physical and catalytic properties of the R. leguminosarum protocatechuate 4,5-dioxygenase were different from the published characteristics of isofunctional enzymes from Pseudomonas paucimobilis and Comamonas testosteroni.Abbreviations P45D
protocatechuate 4,5-dioxygenase
- CAPS
3-Cyclohexylamino]-1-propanesulfonic acid
A preliminary account of this work was presented at the 93rd General Meeting of the American Society for Microbiology, Atlanta, GA, 1993. |
| |
Keywords: | Aromatic catabolism Protocatechuate 4 5-dioxygenase Rhizobium Amino acid composition |
本文献已被 SpringerLink 等数据库收录! |
|