| Literature DB >> 1530847 |
P J White1, J Nairn, N C Price, H G Nimmo, J R Coggins, I S Hunter.
Abstract
The enzyme 3-phosphoglycerate mutase was purified 192-fold from Streptomyces coelicolor, and its N-terminal sequence was determined. The enzyme is tetrameric with a subunit Mr of 29,000. It is 2,3-bisphosphoglycerate dependent and inhibited by vanadate. The gene encoding the enzyme was cloned by using a synthetic oligonucleotide probe designed from the N-terminal peptide sequence, and the complete coding sequence was determined. The deduced amino acid sequence is 64% identical to that of the phosphoglycerate mutase of Saccharomyces cerevisiae and has substantial identity to those of other phosphoglycerate mutases.Entities:
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Year: 1992 PMID: 1530847 PMCID: PMC205734 DOI: 10.1128/jb.174.2.434-440.1992
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490