Chistoserdova, Ludmila V. and Lidstrom, Mary E. (1992) Cloning, Mutagenesis, and Physiological Effect of a Hydroxypyruvate Reductase Gene from Methylobacterium extorquens AM1. Journal of Bacteriology, 174 (1). pp. 71-77. ISSN 0021-9193. http://resolver.caltech.edu/CaltechAUTHORS:20120316-094110842
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The gene encoding the serine cycle hydroxypyruvate reductase of Methylobacterium extorquens AM1 was isolated by using a synthetic oligonucleotide with a sequence based on a known N-terminal amino acid sequence. The cloned gene was inactivated by insertion of a kanamycin resistance gene, and recombination of this insertion derivative with the wild-type gene produced a serine cycle hydroxypyruvate reductase null mutant. This mutant had lost its ability to grow on C-1 compounds but retained the ability to grow on C-2 compounds, showing that the hydroxypyruvate reductase operating in the serine cycle is not involved in the conversion of acetyl coenzyme A to glycine as previously proposed. A second hydroxypyruvate-reducing enzyme with a low level of activity was found in M. extorquens AM1; this enzyme was able to interconvert glyoxylate and glycollate. The gene encoding hydroxypyruvate reductase was shown to be located about 3 kb upstream of two other serine cycles genes encoding phosphoenolpyruvate carboxylase and malyl coenzyme A lyase.
|Additional Information:||© 1992 American Society for Microbiology. Received 2 August 1991. Accepted 25 October 1991. This work was supported by Public Health Service grant GM 36296 from the National Institutes of Health. We are grateful for the helpful discussions of Andrei Chistoserdov and his gift of pAYC61.|
|Official Citation:||Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1. L V Chistoserdova and M E Lidstrom J. Bacteriol. January 1992 174:71-77|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Ruth Sustaita|
|Deposited On:||16 Mar 2012 21:25|
|Last Modified:||16 Mar 2012 21:25|
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