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Serine-Glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris)

1974; Elsevier BV; Volume: 370; Issue: 1 Linguagem: Inglês

10.1016/0005-2744(74)90035-7

1878-1454

Alan I. Carpe, Ivan K. Smith,

Biochemical and Molecular Research

Abstract 1. 1.|The serine-glyoxylate aminotransferase (EC 2.6.1.45) isolated from Phaseolus vulgaris , which catalyzes aminotransferase reactions between serine-glyoxylate and serine-pyruvate, was shown to catalyze the reverse reactions hydroxypyruvate-glycine and hydroxypyruvate-alanine. 2. 2.|The equilibrium constant for the reaction of serine and glyoxylate to form hydroxypyruvate and glycine was between 32 and 119. The K m values for hydroxypyruvate and glycine were 1.1·10 −3 and 1.1·10 −2 M, respectively. The equilibrium constant for the reaction of serine and pyruvate to form hydroxypyruvate and alanine was 43. The K m values for hydroxypyruvate and alanine were 6.3·10 −4 and 2·10 −2 M, respectively. 3. 3.|The reverse reactions were inhibited by low concentrations of hydroxylamine, but were less sensitive to N -ethylmaleimide and p -hydroxymercuribenzoate. The reverse activities were not specifically affected by NH 4 + .