EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
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 |
? |
- |
- |
2.7.1.165 | ADP + (R)-glycerate |
at 32% of the activity with ATP |
Pyrococcus horikoshii |
AMP + 3-phospho-(R)-glycerate |
- |
? |
2.7.1.165 | ADP + (R)-glycerate |
32% of the activity with ATP |
Pyrococcus horikoshii |
AMP + 2-phospho-(R)-glycerate |
- |
? |
2.7.1.165 | ADP + (R)-glycerate |
76% of the activity with GTP |
Sulfurisphaera tokodaii |
AMP + 2-phospho-(R)-glycerate |
- |
? |
2.7.1.165 | ADP + (R)-glycerate |
76% of the activity with GTP |
Sulfurisphaera tokodaii 7 |
AMP + 2-phospho-(R)-glycerate |
- |
? |
2.7.1.165 | ADP + D-glycerate |
76% activity compared to GTP |
Sulfurisphaera tokodaii |
AMP + 2-phospho-D-glycerate |
- |
? |
2.7.1.165 | AMP + (R)-glycerate |
54% of the activity with GTP |
Sulfurisphaera tokodaii |
adenosine + 2-phospho-(R)-glycerate |
- |
? |