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Plant Physiology 52:63-67 (1973)
© 1973 American Society of Plant Biologists

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Articles

Properties of an Aminotransferase of Pea (Pisum sativum L.) 1

Michael E. Matheron and Thomas C. Moore2

a Department of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331

A transaminase (aminotransferase, EC 2.6.1) fraction was partially purified from shoot tips of pea (Pisum sativum L. cv. Alaska) seedlings. With {alpha}-ketoglutarate as co-substrate, the enzyme transaminated the following aromatic amino acids: D,L-tryptophan, D,L-tyrosine, and D,L-phenylalanine, as well as the following aliphatic amino acids: D,L-alanine, D,L-methionine, and D,L-leucine. Of other {alpha}-keto acids tested, pyruvate and oxalacetate were more active than {alpha}-ketoglutarate with D,L-tryptophan. Stoichiometric yields of indolepyruvate and glutamate were obtained with D,L-tryptophan and {alpha}-ketoglutarate as co-substrates. The specific activity was three times higher with D-tryptophan than with L-tryptophan.

2 Author to whom reprint requests should be sent.

1 This study represents part of a thesis presented by Michael E. Matheron to the Graduate School of Oregon State University in partial fulfillment of the requirements for the M.S. degree. The study was supported in part by Grant GB-18494 from the National Science Foundation.






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