Cloning, mutagenesis, and physiological effect of a hydroxypyruvate reductase gene from Methylobacterium extorquens AM1.

Content Provider	Semantic Scholar
Author	Chistoserdova, Ludmila Lidstrom, Mary E.
Copyright Year	1992
Abstract	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.
File Format	PDF HTM / HTML
DOI	10.1128/jb.174.1.71-77.1992
PubMed reference number	1729225
Journal	Medline
Volume Number	174
Issue Number	1
Alternate Webpage(s)	http://authors.library.caltech.edu/29744/1/CHIjbact92.pdf
Alternate Webpage(s)	https://doi.org/10.1128/jb.174.1.71-77.1992
Journal	Journal of bacteriology
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article