EC Number   |
General Information |
Reference |
|---|
    2.4.1.266 | malfunction |
construction of a MSMEG_5084 knock-out mutant. As compared to its wild-type strain, the knock-out mutant strain mutant displays a significantly reduced growth rate at 37°C. Virtual elimination of the de novo production of methylglucose lipopolysaccharides molecules in the mutant |
710353 |
| 2.4.1.266 | physiological function |
enzymes responsible for the transfer of the first glucose residue of methylglucose lipopolysaccharides |
710353 |
| 2.4.1.266 | physiological function |
key enzyme of glucosylglycerate synthesis. Glucosylglycerate is a widespread compatible solute among cyanobacteria. It appears to replace glutamate as an anion to counter monovalent cations in marine picocyanobacteria from N-poor environments |
-, 703481 |
| 2.4.1.266 | physiological function |
key enzyme of glucosylglycerate synthesis. Glucosylglycerate is a widespread solute among cyanobacteria. It appears to replace glutamate as an anion to counter monovalent cations in marine picocyanobacteria from N-poor environments |
703481 |
| 2.4.1.266 | physiological function |
key enzyme that catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria |
706959 |
| 2.4.1.266 | physiological function |
the increased resilience of this pathogen is due, to a great extent, to its complex, polysaccharide-rich, and unusually impermeable cell wall. Enzymes involved in glycosidic bond synthesis represent more than 1% of all ORFs identified from Mycobacterium tuberculosis. One of them is GpgS, a retaining glycosyltransferase with low sequence homology to any other glycosyltransferases of known structure, which has been identified in two species of mycobacteria and shown to be essential for the survival of Mycobacterium tuberculosis |
710352 |
