Purification and properties of a homodimeric protocatechuate 4,5-dioxygenase from Rhizobium leguminosarum |
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Authors: | Yung Pin Chen Charles R. Lovell |
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Affiliation: | (1) Department of Biological Sciences, University of South Carolina, 29208 Columbia, SC, USA |
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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 Km 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 acidA preliminary account of this work was presented at the 93rd General Meeting of the American Society for Microbiology, Atlanta, GA, 1993. |
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Keywords: | Aromatic catabolism Protocatechuate 4,5-dioxygenase Rhizobium Amino acid composition |
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