Chistoserdova, Ludmila V. and Lidstrom, Mary E. (1991) Purification and Characterization of Hydroxypyruvate Reductase from the Facultative Methylotroph Methylobacterium extorquens AM1. Journal of Bacteriology, 173 (22). pp. 7228-7232. ISSN 0021-9193 http://resolver.caltech.edu/CaltechAUTHORS:20120418-153746786
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Hydroxypyruvate reductase was purified to homogeneity from the facultative methylotroph Methylobacterium extorquens AM1. It has a molecular mass of about 71 kDa, and it consists of two identical subunits with a molecular mass of about 37 kDa. This enzyme uses both NADH (K_m = 0.04 mM) and NADPH (K_m = 0.06 mM) as cofactors, uses hydroxypyruvate (K_m = 0.1 mM) and glyoxylate (K_m = 1.5 mM) as the only substrates for the forward reaction, and carries out the reverse reaction with glycerate (K_m = 2.6 mM) only. It was not possible to detect the conversion of glycolate to glyoxylate, a proposed role for this enzyme. Kinetics and inhibitory studies of the enzyme from M. extorquens AM1 suggest that hydroxypyruvate reductase is not a site for regulation of the serine cycle at the level of enzyme activity.
|Additional Information:||© 1991 American Society for Microbiology. Received 28 May 1991. Accepted 10 September 1991. This work was supported by a grant from the Public Health Service National Institutes of Health (GM36296).|
|Official Citation:||Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1. L V Chistoserdova, M E Lidstrom J Bacteriol. 1991 November; 173(22): 7228–7232. PMCID: PMC209229|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Ruth Sustaita|
|Deposited On:||19 Apr 2012 14:52|
|Last Modified:||19 Apr 2012 14:52|
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