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

Yoshikazu Takada, Tomoo Noguchi, Ryo Kido

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish (US)
Pages (from-to)609-616
Number of pages8
JournalLife Sciences
Volume20
Issue number4
DOIs
StatePublished - Feb 15 1977
Externally publishedYes

Fingerprint

diiodophenylpyruvate reductase
Purification
Cytosol
Enzymes
Dogs
Keto Acids
Oxaloacetic Acid
Malate Dehydrogenase
Coenzymes
Isoelectric Point
Pyruvic Acid
NADP
Liver
NAD
Isoenzymes
Brain
Molecular Weight
Molecular weight
Kidney
Substrates

ASJC Scopus subject areas

  • Pharmacology

Cite this

Purification, characterization and identification of aromatic 2-oxo acid reductase. / Takada, Yoshikazu; Noguchi, Tomoo; Kido, Ryo.

In: Life Sciences, Vol. 20, No. 4, 15.02.1977, p. 609-616.

Research output: Contribution to journalArticle

Takada, Yoshikazu ; Noguchi, Tomoo ; Kido, Ryo. / Purification, characterization and identification of aromatic 2-oxo acid reductase. In: Life Sciences. 1977 ; Vol. 20, No. 4. pp. 609-616.
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