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 M(r) of 29,000. It is 2,3-bisphosphoglycerate dependent and inhibited hy 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.
Original language | English |
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Pages (from-to) | 434-440 |
Number of pages | 7 |
Journal | Journal of Bacteriology |
Volume | 174 |
Issue number | 2 |
Publication status | Published - Jan 1992 |
Keywords
- AMINO-ACID SEQUENCE
- SCHIZOSACCHAROMYCES-POMBE
- MOLECULAR-CLONING
- CDNA