EC Number |
Reaction |
Reference |
---|
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
fructose 1,6-diphosphate regulates equilibrium of dimer-tetramer, mechanism of inhibition |
641316 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
glycerone and L-glyceraldehyde can act as acceptors, in some organisms UTP, ITP or GTP can act as donors |
- |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
mechanism |
-, 641322 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
ordered bi bi mechanism with glycerol adding before the magnesium nucleotide and L-glycerol 3-phosphate are released |
641305 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
ordered mechanism |
641287 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
ordered mechanism with glycerol as the first substrate to bind |
641311 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
ping-pong mechanism |
641289, 641292 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
random bi bi mechanism |
641288 |
2.7.1.30 | ATP + glycerol = ADP + sn-glycerol 3-phosphate |
the structure of the TGK-pNPP complex, and structure-guided mutagenesis implicate that enzyme residue T276 is important for the catalysis. The enzyme is a bifunctional kinase/phosphatase. Proposed catalytic mechanism for the phosphatase activity of TbgGK |
760620 |