SCHAAF, PMM and HEIDE, LE and LEISTNER, EW and TANI, Y and KARAS, M and DEUTZMANN, R (1993) PROPERTIES OF ISOCHORISMATE HYDROXYMUTASE FROM FLAVOBACTERIUM-K. JOURNAL OF NATURAL PRODUCTS, 56 (8). pp. 1294-1303. ISSN 0163-3864,
Full text not available from this repository.Abstract
Isochorismate hydroxymutase (isochorismate synthase, E.C. 5.4.99.6) catalyzes the interconversion of chorismic acid [1) and isochorismic acid [2]. The enzyme was extracted from a Flavobacterium K3-15 that overproduces vitamin K2 (i.e., menaquinones) and was purified to homogeneity. The N-terminal amino acid sequence and the mol wt (36,240+/-100 daltons) were determined by ms following SDS PAG electrophoresis. The enzyme was characterized (stability, cofactor requirement, isoelectrical point), and antibodies were raised which showed no cross reactivity with isochorismate hydroxymutase from Escherichia coli and Exterobacter aerogenes 62-1. The kinetic data of the enzyme are different from those observed for the corresponding enzyme from Escherichia coli and Galium mollugo.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ORTHO-SUCCINYLBENZOIC ACID; CELL-SUSPENSION-CULTURES; ESCHERICHIA-COLI; ENTC GENE; BIOSYNTHESIS; SYNTHASE; ENTEROBACTIN; CHORISMATE; SEQUENCE; PROTEINS; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53858 |
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