Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | Streptomyces coelicolor | - |
phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | Streptomyces coelicolor ATCC BAA-471 | - |
phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | Q9L1K2 | - |
- |
Streptomyces coelicolor ATCC BAA-471 | Q9L1K2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | - |
Streptomyces coelicolor | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | acceptor and secondary binding sites are identified. The sugar residues in the acceptor subsites +1 to +5 are oriented such that they disfavor the binding of malto-oligosaccharides that bear branches at their 6-positions, consistent with the known acceptor chain specificity of GlgE. A secondary binding site remote from the catalytic center is identified. This site is capable of binding a branched alpha-glucan and is most likely involved in guiding acceptors toward the donor site because its disruption kinetically compromises the ability of GlgE to extend polymeric substrates | Streptomyces coelicolor | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | - |
Streptomyces coelicolor ATCC BAA-471 | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? | |
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n | acceptor and secondary binding sites are identified. The sugar residues in the acceptor subsites +1 to +5 are oriented such that they disfavor the binding of malto-oligosaccharides that bear branches at their 6-positions, consistent with the known acceptor chain specificity of GlgE. A secondary binding site remote from the catalytic center is identified. This site is capable of binding a branched alpha-glucan and is most likely involved in guiding acceptors toward the donor site because its disruption kinetically compromises the ability of GlgE to extend polymeric substrates | Streptomyces coelicolor ATCC BAA-471 | phosphate + [(1->4)-alpha-D-glucosyl]n+2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase | - |
Streptomyces coelicolor |
maltosyltransferase GlgE | - |
Streptomyces coelicolor |
General Information | Comment | Organism |
---|---|---|
drug target | the enzyme has been genetically validated as a target for tuberculosis therapies | Streptomyces coelicolor |
metabolism | the enzyme is involved inx02alpha-glucan biosynthesis in bacteria | Streptomyces coelicolor |