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. 1973 Jul;52(1):63–67. doi: 10.1104/pp.52.1.63

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

Michael E Matheron a, Thomas C Moore a,2
PMCID: PMC366439  PMID: 16658501

Abstract

A transaminase (aminotransferase, EC 2.6.1) fraction was partially purified from shoot tips of pea (Pisum sativum L. cv. Alaska) seedlings. With α-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 α-keto acids tested, pyruvate and oxalacetate were more active than α-ketoglutarate with d,l-tryptophan. Stoichiometric yields of indolepyruvate and glutamate were obtained with d,l-tryptophan and α-ketoglutarate as co-substrates. The specific activity was three times higher with d-tryptophan than with l-tryptophan.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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