PMID: 2114288Jun 20, 1990Paper

Purification and characterization of serine-glyoxylate aminotransferase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2

European Journal of Biochemistry
Yoshikazu IzumiH Yamada

Abstract

Serine--glyoxylate aminotransferase was purified to complete homogeneity from a serine-producing methylotrophic bacterium, Hyphomicrobium methylovorum GM2, which possesses the serine pathway. This is the first microbial serine--glyoxylate aminotransferase to be purified. The enzyme has a molecular mass of about 140 kDa and consists of four subunits of identical mass, i.e. 40 kDa. The holoenzyme exhibited absorption maxima at 282 nm and 408 nm, and a shoulder at about 315-345 nm in potassium phosphate pH 7.0; it contained 4 mol pyridoxal 5'-phosphate/mol enzyme. Isoelectric focusing showed that the enzyme had a pI value of 6.9. The Km values for glyoxylate and L-serine were 0.23 mM and 4.98 mM, respectively, and the enzyme showed high specificity for these substrates. The transamination between glyoxylate and L-serine seemed to be nearly irreversible. These data indicated that this serine--glyoxylate aminotransferase plays an essential role in methanol assimilation through the serine pathway in H. methylovorum GM2.

References

Feb 1, 1977·The Biochemical Journal·F GannonK M Jones
Aug 29, 1986·Biochemical and Biophysical Research Communications·S S MiyazakiH Yamada
Nov 1, 1968·Journal of Bacteriology·L AlföldiE Kerekes
Apr 1, 1970·Canadian Journal of Biochemistry·B L BrockJ King
Jun 1, 1982·The Journal of General Virology·D H GildenY Becker
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May 1, 1963·The Biochemical Journal·P J Large, J R Quayle

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Citations

Jul 1, 1993·Applied Microbiology and Biotechnology·Y IzumiT Tanabe
Jul 4, 2012·Acta Crystallographica. Section D, Biological Crystallography·Christopher SayerJennifer Littlechild
Aug 5, 2004·Journal of Bacteriology·Haruhiko SakurabaToshihisa Ohshima
Aug 14, 2015·Journal of Molecular Recognition : JMR·Surabhi Maheshwari, Michal Brylinski

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