Partial Purification and Properties of Lathyrine Synthase.

J, Brown, E. G. and Mohamad, (1994) Partial Purification and Properties of Lathyrine Synthase. Phytochemistry, 36 (2). pp. 285-287.

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The enzyme catalysing the simultaneous decarboxylation of 2-amino-4-carboxypyrimidine and its condensation with serine to form<span style=\"FONT-WEIGHT: bold; COLOR: #ff0000\"> lathyrine</span> [&beta;-(2-aminopyrimidin-4-yl)alanine] has been partially purified (150-fold) by selective heat denaturation, fractionation with ammonium sulphate, and affinity chromatography on a column of avidin (monomeric)-agarose. In addition to a requirement for pyridoxal 5-monophosphate, the enzyme is stimulated by biotin and inhibited by avidin. It exhibits a bimodal pH optimum curve with a major peak at pH 4.5 and a secondary peak at pH 7.2. CoA, ATP and a range of metal ions were without effect. The activity of the enzyme was assayed by incorporation of [3-<sup>14</sup>C]serine into<span style=\"FONT-WEIGHT: bold; COLOR: #ff0000\"> lathyrine</span>, isolated by sequential chromatography and electrophoresis

Item Type: Article
Uncontrolled Keywords: Lathyrus tingitanus, Leguminosae, lathyrine, pyrimidines, non-protein amino acids.
Subjects: Q Science
Depositing User: MR. ADNAN YAHYA
Date Deposited: 24 Apr 2008
Last Modified: 06 Jun 2011

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