An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization.

An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Research Abstract Details 

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An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Abstract Text:

K Packdibamrung,H Misono,M Harada,S Nagata,S Nagasaki,

An inducible NADP(+)-dependent D-phenylserine dehydrogenase [EC 1.1.1.-], which catalyzes the oxidation of the hydroxyl group of D-threo-beta-phenylserine, was purified to homogeneity from a crude extract of Pseudomonas syringae NK-15 isolated from soil. The enzyme consisted of two subunits identical in molecular weight (about 31,000). In addition to D-threo-beta-phenylserine, it utilized D-threo-beta-thienylserine, D-threo-beta-hydroxynorvaline, and D-threonine as substrates but was inert towards other isomers of beta-phenylserine and threonine. It showed maximal activity at pH 10.4 for the oxidation of D-threo-beta-phenylserine, and it required NADP+ as a natural coenzyme. NAD+ showed a slight coenzyme activity. The enzyme was inhibited by p-chloromercuribenzoate, HgCl2, and monoiodoacetate but not by the organic acids such as tartronate. The Michaelis constants for D-threo-beta-phenylserine and NADP+ were 0.44 mM and 29 microM, respectively. The N-terminal 27 amino acids sequence was determined. It suggested that the NADP(+)-binding site was located in the N-terminal region of the enzyme.

An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Publishing Authors By Initials

K Packdibamrung,H Misono,M Harada,S Nagata,S Nagasaki,

For similar amino acids, peptides, and proteins: amino acids: amino acids, essential: threonine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, essential: threonine research

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An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 114

Page Numbers: 930-5

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1993

An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Keywords Mesh Terms:

KEYWORDS: Threonine

MESH TERMS: analogs & derivatives

Chemical & Substance for Abstract: An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization. Information

Substance Name: NADPH Dehydrogenase

Registry Number: EC 1.6.99.1

Grant and Affiliation Information for An inducible NADP(+)-dependent D-phenylserine dehydrogenase from Pseudomonas syringae NK-15: purification and biochemical characterization.

AFFILIATION: Department of Bioresources Science, Kochi University.

Country: JAPAN

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MEDLINETA: J Biochem

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