Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity.

Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Research Abstract Details 

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Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Abstract Text:

Y Asada,Y Sawa,K Tanizawa,K Soda,

L-Kynurenine aminotransferase [L-kynurenine:2-oxoglutarate aminotransferase (cyclizing), EC 2.6.1.7] has been purified to homogeneity and crystallized from cell-free extracts of a yeast, Hansenula schneggii, grown in a medium containing L-tryptophan as an inducer. The enzyme has a molecular weight of about 100,000 and consists of two subunits identical in molecular weight (52,000). The enzyme exhibits absorption maxima at 280, 335, and 430 nm, and contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme. The enzyme-bound pyridoxal 5'-phosphate shows negative circular dichroic extrema, in contrast with other pyridoxal 5'-phosphate acting on L-amino acids. In addition to L-kynurenine and alpha-ketoglutarate, which are the most preferred substrates, a large number of L-amino acids and alpha-keto acids can serve as substrates; the extremely broad substrate specificity is the most characteristic feature of this yeast enzyme. The enzyme activity is significantly affected by both carbonyl and sulfhydryl reagents. Certain dicarboxylic acids such as adipate and pimelate act as competitive inhibitors. Addition of various substrate amino acids to the culture medium results in the inductive formation of aminotransferases which are immunochemically indistinguishable from L-kynurenine aminotransferase.

Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Publishing Authors By Initials

Y Asada,Y Sawa,K Tanizawa,K Soda,

For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tryptophan research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tryptophan research

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Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 99

Page Numbers: 1101-10

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1986

Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Keywords Mesh Terms:

KEYWORDS: Tryptophan

MESH TERMS: physiology

Chemical & Substance for Abstract: Purification and characterization of yeast L-kynurenine aminotransferase with broad substrate specificity. Information

Substance Name: Lyases

Registry Number: EC 4.-

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Country: JAPAN

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MEDLINETA: J Biochem

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