Purification, characterization and identification of aromatic 2-oxo acid reductase

Yoshikazu Takada; Tomoo Noguchi; Ryo Kido

doi:10.1016/0024-3205(77)90463-5

Purification, characterization and identification of aromatic 2-oxo acid reductase

Yoshikazu Takada, Tomoo Noguchi, Ryo Kido

Research output: Contribution to journal › Article › peer-review

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Abstract

Aromatic 2-oxo acid reductase was purified to homogeneity from the cytosol of dog heart. The purified enzyme utilized various 2-oxo acids as substrates in the following order of activity: oxaloacetate > 3,5-diiodo-4-hydroxyphenylpyruvate > indolepyruvate > phenylpyruvate. Little or no activity was detected with glyoxylate, pyruvate, hydroxypyruvate, 2-oxoglutarate and 2-oxoadipate. NADH was active as coenzyme but not NADPH. The enzyme has an isoelectric point of 5.4 and is probably composed of two identical subunits with a molecular weight of approx. 40000. Evidence was presented that aromatic 2-oxo acid reductase is identical with one of the cytosol malate dehydrogenase isoenzymes. The enzyme was also found in the brain, kidney and liver of dog.

Original language	English
Pages (from-to)	609-616
Number of pages	8
Journal	Life Sciences
Volume	20
Issue number	4
DOIs	https://doi.org/10.1016/0024-3205(77)90463-5
Publication status	Published - Feb 15 1977
Externally published	Yes

ASJC Scopus subject areas

General Pharmacology, Toxicology and Pharmaceutics
General Biochemistry,Genetics and Molecular Biology

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10.1016/0024-3205(77)90463-5

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title = "Purification, characterization and identification of aromatic 2-oxo acid reductase",

abstract = "Aromatic 2-oxo acid reductase was purified to homogeneity from the cytosol of dog heart. The purified enzyme utilized various 2-oxo acids as substrates in the following order of activity: oxaloacetate > 3,5-diiodo-4-hydroxyphenylpyruvate > indolepyruvate > phenylpyruvate. Little or no activity was detected with glyoxylate, pyruvate, hydroxypyruvate, 2-oxoglutarate and 2-oxoadipate. NADH was active as coenzyme but not NADPH. The enzyme has an isoelectric point of 5.4 and is probably composed of two identical subunits with a molecular weight of approx. 40000. Evidence was presented that aromatic 2-oxo acid reductase is identical with one of the cytosol malate dehydrogenase isoenzymes. The enzyme was also found in the brain, kidney and liver of dog.",

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AU - Takada, Yoshikazu

AU - Noguchi, Tomoo

AU - Kido, Ryo

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Y1 - 1977/2/15

N2 - Aromatic 2-oxo acid reductase was purified to homogeneity from the cytosol of dog heart. The purified enzyme utilized various 2-oxo acids as substrates in the following order of activity: oxaloacetate > 3,5-diiodo-4-hydroxyphenylpyruvate > indolepyruvate > phenylpyruvate. Little or no activity was detected with glyoxylate, pyruvate, hydroxypyruvate, 2-oxoglutarate and 2-oxoadipate. NADH was active as coenzyme but not NADPH. The enzyme has an isoelectric point of 5.4 and is probably composed of two identical subunits with a molecular weight of approx. 40000. Evidence was presented that aromatic 2-oxo acid reductase is identical with one of the cytosol malate dehydrogenase isoenzymes. The enzyme was also found in the brain, kidney and liver of dog.

AB - Aromatic 2-oxo acid reductase was purified to homogeneity from the cytosol of dog heart. The purified enzyme utilized various 2-oxo acids as substrates in the following order of activity: oxaloacetate > 3,5-diiodo-4-hydroxyphenylpyruvate > indolepyruvate > phenylpyruvate. Little or no activity was detected with glyoxylate, pyruvate, hydroxypyruvate, 2-oxoglutarate and 2-oxoadipate. NADH was active as coenzyme but not NADPH. The enzyme has an isoelectric point of 5.4 and is probably composed of two identical subunits with a molecular weight of approx. 40000. Evidence was presented that aromatic 2-oxo acid reductase is identical with one of the cytosol malate dehydrogenase isoenzymes. The enzyme was also found in the brain, kidney and liver of dog.

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Purification, characterization and identification of aromatic 2-oxo acid reductase

Abstract

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