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Isolation and Properties of Aromatic -Keto Acid Reductase

From the ¹ From the Department of Pharmacology, New York University Medical School, New York, New York 10016

An enzyme which catalyzes the reduction of aromatic -keto acids to phenyllactic acids has been isolated from beef and dog heart. This enzyme has been designated aromatic -keto acid reductase.

Reduced diphosphopyridine nucleotide is a required cofactor for aromatic -keto acid reductase activity.

Substrates for aromatic -keto acid reductase include 3,5-diiodo-p-hydroxyphenylpyruvic acid, p-hydroxyphenylpyruvic acid, and phenylpyruvic acid. 3,5-Diiodo-p-hydroxyphenylpyruvic acid has a high affinity for the enzyme (K_m of 4.3 x 10^-5 m).

The enzyme is present in many mammalian tissues. These include heart, skeletal muscle, kidney, adrenal, liver, thyroid, and blood.

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