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Results 1 - 9 of 9
EC Number Reaction Commentary Reference
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate fructose 1,6-diphosphate regulates equilibrium of dimer-tetramer, mechanism of inhibition 641316
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + 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 -
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate mechanism -, 641322
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + 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
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate ordered mechanism 641287
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate ordered mechanism with glycerol as the first substrate to bind 641311
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate ping-pong mechanism 641289, 641292
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + glycerol = ADP + sn-glycerol 3-phosphate random bi bi mechanism 641288
Show all pathways known for 2.7.1.30Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.30ATP + 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
Results 1 - 9 of 9