Purification and properties of an asparagine aminotransferase from Pisum sativum leaves

Archives of Biochemistry and Biophysics
R J Ireland, K W Joy

Abstract

The enzyme responsible for the transamination of L-asparagine in pea leaves has been partially purified. It appears to be the same protein as the serine-glyoxylate aminotransferase. It is able to use serine or asparagine as amino donors and pyruvate or glyoxylate as amino acceptors. The reaction is reversible but the equilibrium is toward glycine or alanine production. The favored substrates are serine and glyoxylate: serine shows competitive inhibition toward asparagine, as does pyruvate toward glyoxylate. Substrate interaction and product inhibition patterns are consistent with a ping-pong mechanism. The enzyme has a pH optimum at 8.1. Gel filtration indicates a Mr of 105,000. Inhibition was caused by aminoxyacetate and hydroxylamine, but the enzyme was unaffected by isonicotinic acid hydrazide. The apoenzyme was resolved and was inactive: addition of pyridoxal 5'-phosphate restored 85% of the original activity.

References

Jun 1, 1988·Plant Physiology·D G Brunk, D Rhodes
Aug 17, 1987·European Journal of Biochemistry·P A Der Garabedian, J J Vermeersch
Mar 13, 2003·The Plant Journal : for Cell and Molecular Biology·Daisuke IgarashiChieko Ohsumi
Feb 1, 2008·Acta Biochimica Et Biophysica Sinica·Maria Kendziorek, Andrzej Paszkowski

Citations

Jul 8, 1969·Biochimica Et Biophysica Acta·Z H Verjee, D F Evered
Sep 18, 1980·Biochimica Et Biophysica Acta·S W HuiP L Yeagle
Mar 1, 1981·Planta·R J Ireland, K W Joy

Related Concepts

Asparagine
Apoenzymes
Pyruvate Measurement
Serine-glyoxylate aminotransferase
Pyridoxal Phosphate
Tachigalia
Glycine
Etiology
Pyruvate
Glycine (Plant)

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