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

Yoshikazu Takada, Tomoo Noguchi, Ryo Kido

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1 Scopus citations


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 languageEnglish (US)
Pages (from-to)609-616
Number of pages8
JournalLife Sciences
Issue number4
StatePublished - Feb 15 1977
Externally publishedYes

ASJC Scopus subject areas

  • Pharmacology


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