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Purification and Characterization of Hydroxypyruvate Reductase from the Facultative Methylotroph Methylobacterium extorquens AM1

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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Abstract

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.


Item Type:Article
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC209229/PubMed Central IDUNSPECIFIED
http://jb.asm.org/content/173/22/7228PublisherUNSPECIFIED
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).
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Funding AgencyGrant Number
NIH Public Health ServiceGM36296
Record Number:CaltechAUTHORS:20120418-153746786
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20120418-153746786
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.
ID Code:30184
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:19 Apr 2012 14:52
Last Modified:19 Apr 2012 14:52

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