EC Number   |
General Information |
Reference |
|---|
   2.4.99.16 | drug target |
the enzyme has been genetically validated as a target for tuberculosis therapies |
-, 759476 |
| 2.4.99.16 | malfunction |
a constructed DELTAglgE null mutant strain was viable but shows a delayed developmental phenotype when grown on maltose, giving less cell mass and delayed sporulation. Pre-spore cells and spores of the mutant are frequently double the length of those of the wild-type, implying impaired cross-wall formation, and spores show reduced tolerance to stress. The mutant accumulates alpha-maltose 1-phosphate and maltose but no alpha-glucan |
-, 759739 |
| 2.4.99.16 | metabolism |
the enzyme catalyzes the last step in the conversion of trehalose to glycogen transfering maltose from maltose 1-phosphate to glycogen. Trehalose synthase, maltokinase, and GMPMT represent an additional pathway of glycogen synthesis using trehalose as the source of glucose |
-, 717816 |
| 2.4.99.16 | metabolism |
the enzyme is involved inx02alpha-glucan biosynthesis in bacteria |
-, 759476 |
| 2.4.99.16 | metabolism |
the following assembly mechanism is proposed. Polymer synthesis starts with GlgE and its donor substrate, alpha-maltose 1-phosphate, yielding a linear oligomer with a degree of polymerization (of about 16) sufficient for GlgB to introduce a branch. Branching involves strictly intrachain transfer to generate a C chain (the only constituent chain to retain its reducing end), which now bears an A chain (a nonreducing end terminal branch that does not itself bear a branch). GlgE preferentially extends A chains allowing GlgB to act iteratively to generate new A chains emanating from B chains (nonterminal branches that themselves bear a branch). Although extension and branching occur primarily with A chains, the other chain types are sometimes extended and branched such that some B chains (and possibly C chains) bear more than one branch |
-, 758790 |
