Abstract
The transaminations of serine, glutamate and alanine with glyoxylate have been measured over a range of substrate concentrations in pea leaf extracts and related to glycollate oxidation at pH 8.8. In crude homogenates and at 20 mM amino acid and 5 mM glyoxylate, each transamination exceeded glycollate oxidation and the greatest reaction was with alanine. However (in dialysed extracts) transamination with serine required a lower concentration of amino acid than with glutamate or alanine. It was concluded that in homogenates supplied with 0.5 mM glyoxylate (near-saturating), transamination with either 2 mM serine or 2 mM alanine would be substantially greater than with 2 mM glutamate. Inhibitions of alanine transamination by serine and glutamate were observed, together with the converse effects, but only at high concentrations of the inhibiting compounds. The possible role of alanine as a third amino group donor to glyoxylate in the photorespiratory cycle is discussed.
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