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Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide
- Source :
- Journal of Bacteriology. August, 1994, Vol. 176 Issue 15-16, p4851, 7 p.
- Publication Year :
- 1994
-
Abstract
- Purification and characterization of phosophomannomutase (PMM) derived from Pseudomonas aeruginosa show that the PMM enzyme affects the biosynthesis of alginate and lipopolysaccharide by using both phosphomannose and phosphoglucose as substrates. PMM catalyzes the interconversion of mannose 1-phosphate, mannose 6-phosphate, glucose 1-phosphate and glucose 6-phosphate and the conversion of ribose 1-phosphate and 2-deoxyglucose 6-phosphate. The enzymes PMM and phosphoglucomutase do not affect the nonmucoid algC mutant strain 8858 and the LPS-rough algC mutant strain AK1012.
- Subjects :
- Pseudomonas aeruginosa -- Research
Endotoxins -- Research
Biological sciences
Subjects
Details
- ISSN :
- 00219193
- Volume :
- 176
- Issue :
- 15-16
- Database :
- Gale General OneFile
- Journal :
- Journal of Bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.16484266