Properties of isochorismate hydroxymutase from Flavobacterium K3-15.
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 Enterobacter aerogenes 62-1. The kinetic data of the enzyme are different from those observed for the corresponding enzyme from Escherichia coli and Galium mollugo.
Schaaf
P M
PM
Institut für Pharmazeutische Biologie, Rheinischen Friedrich-Wilhelms-Universität Bonn, Germany.
Heide
L E
LE
Leistner
E W
EW
Tani
Y
Y
Karas
M
M
Deutzmann
R
R
D000595:Amino Acid Sequence; D000907:Antibodies, Bacterial / Q000096:biosynthesis / Q000276:immunology; D000918:Antibody Specificity; D001426:Bacterial Proteins / Q000737:chemistry*; D015153:Blotting, Western; D002827:Chorismic Acid / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D005417:Flavobacterium / Q000737:chemistry / Q000201:enzymology*; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight
D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D007535:Isomerases; D019751:Intramolecular Transferases; C058486:isochorismate synthase; D002827:Chorismic Acid