EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.7.1.165 | more |
AMP is not a substrate |
Pyrococcus horikoshii |
? |
- |
? |
2.7.1.165 | more |
ATP can be partially replaced by GTP, CTP, TTP and UTP (16%, 20%, 16%, and 10% activity, respectively) |
Thermoproteus tenax |
? |
- |
? |
2.7.1.165 | more |
GTP, CTP, UTP, D-glucose, D-gluconate, glycerol, D-fructose, DL-glyceraldehyde, D-ribose, D-xylose, 2-phospho-D-glycerate, 3-phospho-D-glycerate, and L-tartrate are no substrates |
Thermoplasma acidophilum |
? |
- |
? |
2.7.1.165 | more |
L-glycerate, galactonate, gluconate, malate, pyruvate, lactate, glyceraldehyde, glycerol, serine, 3-phosphoglycerate, ADP, diphosphate, polyphosphate, and glyceraldehyde 3-phosphate are no substrates |
Thermoproteus tenax |
? |
- |
? |
2.7.1.165 | more |
the enzyme shows highest activity with D-glycerate (100%), and lower activity (34%) with L-glycerate |
Picrophilus torridus |
? |
- |
? |
2.7.1.165 | more |
no activity is observed with ADP, diphosphate and polyphosphates |
Thermoproteus tenax |
? |
- |
? |
2.7.1.165 | more |
biocatalytic phosphorylations catalyzed by recombinant glycerate-2-kinase are detected with quantitative 31P NMR spectroscopy using a phosphoenolpyruvate (PEP)/pyruvate kinase system for ATP regeneration, starting with racemic and the enantiopure D- and L-glycerate as substrate. Nearly 100% conversion of D-glycerate to D-glycerate-2-phosphate is observed. No activity with pure L-glycerate as substrate, DL-glycerate gives a 50% conversion with excellent enantioselectivity. Optimization of the reaction system for the biocatalytic phosphorylation of D-glyceric acid, upscaling, overview |
Thermotoga maritima |
? |
- |
- |
2.7.1.165 | more |
biocatalytic phosphorylations catalyzed by recombinant glycerate-2-kinase are detected with quantitative 31P NMR spectroscopy using a phosphoenolpyruvate (PEP)/pyruvate kinase system for ATP regeneration, starting with racemic and the enantiopure D- and L-glycerate as substrate. Nearly 100% conversion of D-glycerate to D-glycerate-2-phosphate is observed. No activity with pure L-glycerate as substrate, DL-glycerate gives a 50% conversion with excellent enantioselectivity. Optimization of the reaction system for the biocatalytic phosphorylation of D-glyceric acid, upscaling, overview |
Thermotoga maritima DSM 3109 |
? |
- |
- |
2.7.1.165 | more |
biocatalytic phosphorylations catalyzed by recombinant glycerate-2-kinase are detected with quantitative 31P NMR spectroscopy using a phosphoenolpyruvate (PEP)/pyruvate kinase system for ATP regeneration, starting with racemic and the enantiopure D- and L-glycerate as substrate. Nearly 100% conversion of D-glycerate to D-glycerate-2-phosphate is observed. No activity with pure L-glycerate as substrate, DL-glycerate gives a 50% conversion with excellent enantioselectivity. Optimization of the reaction system for the biocatalytic phosphorylation of D-glyceric acid, upscaling, overview |
Thermotoga maritima ATCC 43589 |
? |
- |
- |
2.7.1.165 | more |
biocatalytic phosphorylations catalyzed by recombinant glycerate-2-kinase are detected with quantitative 31P NMR spectroscopy using a phosphoenolpyruvate (PEP)/pyruvate kinase system for ATP regeneration, starting with racemic and the enantiopure D- and L-glycerate as substrate. Nearly 100% conversion of D-glycerate to D-glycerate-2-phosphate is observed. No activity with pure L-glycerate as substrate, DL-glycerate gives a 50% conversion with excellent enantioselectivity. Optimization of the reaction system for the biocatalytic phosphorylation of D-glyceric acid, upscaling, overview |
Thermotoga maritima JCM 10099 |
? |
- |
- |