EC Number   |
General Information |
Reference |
|---|
   2.7.1.175 | more |
enzyme complex structure analysis and location of active sites, overview |
-, 759499 |
| 2.7.1.175 | evolution |
genetic environment of the mak gene in different organisms. Organization of the region containing the mak gene, overview |
717432 |
| 2.7.1.175 | metabolism |
involvement of maltose-1-phosphate in the regulation of sugar metabolism in Escherichia coli |
717432 |
| 2.7.1.175 | physiological function |
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate |
717739 |
| 2.7.1.175 | more |
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview |
-, 737320 |
| 2.7.1.175 | physiological function |
the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis, is coated by an alpha-glucan-containing capsule that has been implicated in persistence. Maltokinase Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2. Synthesis of alpha-glucan in mycobacteria involves the heterooctameric complex in the GlgE pathway. The complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients |
-, 737320 |
| 2.7.1.175 | evolution |
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview |
-, 739666 |
| 2.7.1.175 | metabolism |
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan |
-, 739666 |
| 2.7.1.175 | metabolism |
the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose |
-, 717816 |
| 2.7.1.175 | metabolism |
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2 |
-, 759499 |
