Enzymatic assay for L-serine and glyoxylate involving the enzymes in the serine pathway of a methylotroph.
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.[1]References
- Enzymatic assay for L-serine and glyoxylate involving the enzymes in the serine pathway of a methylotroph. Yoshida, T., Mitsunaga, T., Yamada, H., Izumi, Y. Anal. Biochem. (1993) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg