type	Journal Article
authors	Yoshida, T.; Mitsunaga, T.; Yamada, H.; Izumi, Y.
title	Enzymatic assay for L-serine and glyoxylate involving the enzymes in the serine pathway of a methylotroph
journal	Anal Biochem
Activity	2.6.1.45
ui	93198996
year	(1993)
volume	208
number	2
pages	296-9.
keywords	Alcohol Oxidoreductases/isolation & purification
abstract	An easy, rapid, and accurate enzymatic assay method for L-serine was established involving two enzymes, serine-glyoxylate aminotransferase (SGAT, EC 2.6.1.45) and hydroxypyruvate reductase (HPR, EC 1.1.1.81), in the serine pathway of the methylotrophic bacterium, Hyphomicrobium methylovorum (IFO 14180), from which they were purified. This method consists of two reaction steps: the first is the nearly irreversible transamination of L-serine and glyoxylate by SGAT, and the second is the HPR reaction involving NADH, which comprises the absolutely irreversible reduction of hydroxypyruvate derived from L-serine by SGAT. The amounts of L-serine were determined spectrophotometrically as the decrease in the amount of NADH. When the values determined with the present enzymatic method were compared with those obtained with an amino acid analyzer, the correlation coefficient was found to be 0.9963. This method can also be applied to the assaying of glyoxylate.
last changed	2002/11/12 16:17