EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.4.1.342 | structure at 1.9 A resolution. GlgM shares a GT-B fold with bacterial glycogen synthases | Mycolicibacterium smegmatis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.342 | D-glucose 1-phosphate | substrate inhibition above 4 mM | Mycolicibacterium smegmatis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.342 | Mycolicibacterium smegmatis | A0R2E2 | - |
- |
2.4.1.342 | Mycolicibacterium smegmatis ATCC 700084 | A0R2E2 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.342 | additional information | enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity | Mycolicibacterium smegmatis | ? | - |
- |
|
2.4.1.342 | additional information | enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.342 | glgM | - |
Mycolicibacterium smegmatis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.342 | 40 | - |
- |
Mycolicibacterium smegmatis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.342 | 6 | - |
- |
Mycolicibacterium smegmatis |