Glutamate dehydrogenase from Pseudomonas
AssigneeToyo Boseki Kabushiki Kaisha
InventorsNoriyuki Hongo, Shizuo Hattori, Kazumi Yamamoto, Shinichi Teshima, Yoshihisa Kawamura
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Abstract
A novel glutamate dehydrogenase is derived from the genus Pseudomonas and is specific to L-glutamic acid, requires NAD.sup.+ and NADH as coenzymes, does not act on NADP.sup.+ and NADPH, has an optimum pH 10.5-11.5 (oxidative deamination), a pH stability of 5-10 (at 25.degree. C.; 20 hours), an optimum temperature of about 60.degree. C. (oxidative deamination) and a molecular weight of about 280,000 (gel filtration) or about 41,000 (SDS-PAGE) and is not activated by ADP.
Claims5
An isolated, purified, water soluble glutamate dehydrogenase produced by Pseudomonas sp. 433-3 having the following physicochemical properties;
- (a) it catalyzes the following reaction
- L-Glutamic acid+H.sub.2 O+NAD.sup.+ =.alpha.-Ketoglutaric acid+NH.sub.3 +NADH;
- (b) it has a substrate specificity to L-glutamic acid;
- it requires NADP.sup.+ and NADH as coenzymes and does not act on NADP.sup.+ and NADPH;
- (c) it is thermally stable up to about 60.degree. C. at a pH of 8.3 for ten minutes;
- and
- (d) it is not activated by ADP.
Dependencies are inferred from the claim text.