2.7.1.165: glycerate 2-kinase
This is an abbreviated version!
For detailed information about glycerate 2-kinase, go to the full flat file.
Word Map on EC 2.7.1.165
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2.7.1.165
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thermoacidophilic
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synthesis
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entner-doudoroff
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non-phosphorylative
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homodimeric
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picrophilus
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thermoplasma
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sulfolobus
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2-keto-3-deoxygluconate
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torridus
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archaea
- 2.7.1.165
-
thermoacidophilic
- synthesis
-
entner-doudoroff
-
non-phosphorylative
-
homodimeric
-
picrophilus
- thermoplasma
- sulfolobus
- 2-keto-3-deoxygluconate
- torridus
- archaea
Reaction
Synonyms
2-PGA forming glycerate kinase, class II GK, class II glycerate kinase, D-glycerate 2-kinase, D-glycerate kinase, D-glycerate-2-kinase, EcoGK1, garK, GCK, glxK, glycerate kinase, glycerate kinase (2-phosphoglycerate forming), Glyctk, GLYK, More, slr1840, Sso-GK, SSO0666, SynGK, Ta0453, TM1585, TM_1585
ECTree
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Substrates Products
Substrates Products on EC 2.7.1.165 - glycerate 2-kinase
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REACTION DIAGRAM
ADP + (R)-glycerate
AMP + 3-phospho-(R)-glycerate
at 32% of the activity with ATP
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-
?
ADP + D-glycerate
AMP + 2-phospho-D-glycerate
76% activity compared to GTP
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-
?
AMP + (R)-glycerate
adenosine + 2-phospho-(R)-glycerate
54% of the activity with GTP
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-
?
AMP + D-glycerate
adenosine + 2-phospho-D-glycerate
54% activity compared to GTP
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-
?
CTP + D-glycerate
CDP + 2-phospho-D-glycerate
87% activity compared to GTP
-
-
?
diphosphate + (R)-glycerate
phosphate + 3-phospho-(R)-glycerate
at 112% of the activity with ATP
-
-
?
diphosphate + D-glycerate
phosphate + 2-phospho-D-glycerate
63% activity compared to GTP
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-
?
GTP + D-glycerate
GDP + 2-phospho-D-glycerate
100% activity towards GTP
-
-
?
TTP + (R)-glycerate
TDP + 2-phospho-(R)-glycerate
16% of the activity with ATP
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-
?
UTP + D-glycerate
UDP + 2-phospho-D-glycerate
81% activity compared to GTP
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-
?
AMP + 2-phospho-(R)-glycerate
32% of the activity with ATP
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-
?
ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
76% of the activity with GTP
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-
?
ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
76% of the activity with GTP
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
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enzymes in the (D)-glucarate/galactarate catabolic pathway
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
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no activity with (S)-glycerate
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
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-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
key enzyme in the Entner-Doudoroff pathway in archaea
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
92% of the activity with GTP
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
key enzyme in the Entner-Doudoroff pathway in archaea
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
92% of the activity with GTP
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-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
enzyme of the branched Entner-Doudoroff pathway
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-
?
ADP + 3-phospho-(R)-glycerate
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activity towards L-glycerate is 13% of that towards D-glycerate
2-phosphoglycerate
ir
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
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2-phosphoglycerate
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
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2-phosphoglycerate
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid
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-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
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-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid
-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid
-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
specific substrate
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
the enzyme is specific for D-glycerate. The enzyme shows cooperativity by D-glycerate and ATP. A good fit achieved from the kinetic model to the experimental data suggests a mechanism where two glycerate molecules bind to glycerate kinase and are converted to product, while a third binding site appears to be inhibitory. The model suggests that the inhibition appears to be due to the formation of an additional complex with very low activity at 80°C
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
specific substrate
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. The glycerate kinase, with its unusual regulatory properties, seems to play a major role in controlling the flux between the glycolytic nonphosphorylative Entner-Doudoroff and the glycolytic/gluconeogenetic semiphosphorylative Entner-Doudoroff pathway
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
the enzyme is specific for D-glycerate. The enzyme shows cooperativity by D-glycerate and ATP. A good fit achieved from the kinetic model to the experimental data suggests a mechanism where two glycerate molecules bind to glycerate kinase and are converted to product, while a third binding site appears to be inhibitory. The model suggests that the inhibition appears to be due to the formation of an additional complex with very low activity at 80°C
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
92% activity compared to GTP
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-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
no activity with DL-glyceraldehyde, 2-phospho-D-glycerate, 3-phospho-D-glycerate or L-tartrate. Activity with D-gluconate or glycerol at 5% of the activity compared to D-glycerate. Specificity for ATP as a phosphate donor. GTP, CTP, and UTP exhibit 0~4% of the activity of ATP
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-
?
CDP + 2-phospho-(R)-glycerate
73% of the activity with ATP
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-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
87% of the activity with GTP
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-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
87% of the activity with GTP
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-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
16% of the activity with ATP
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-
?
CDP + 3-phospho-(R)-glycerate
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at 59% of the activity with ATP
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-
?
CTP + (R)-glycerate
CDP + 3-phospho-(R)-glycerate
at 73% of the activity with ATP
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-
?
phosphate + 2-phospho-(R)-glycerate
112% of the activity with ATP
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-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
63% of the activity with ATP
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-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
63% of the activity with ATP
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-
?
GDP + 2-phospho-(R)-glycerate
64% of the activity with ATP
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-
?
GTP + (R)-glycerate
GDP + 2-phospho-(R)-glycerate
20% of the activity with ATP
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-
?
GDP + 3-phospho-(R)-glycerate
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at 59% of the activity with ATP
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-
?
GTP + (R)-glycerate
GDP + 3-phospho-(R)-glycerate
at 64% of the activity with ATP
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-
?
UDP + 2-phospho-(R)-glycerate
29% of the activity with ATP
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-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
81% of the activity with GTP
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-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
10% of the activity with ATP
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-
?
UDP + 3-phospho-(R)-glycerate
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at 64% of the activity with ATP
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?
UTP + (R)-glycerate
UDP + 3-phospho-(R)-glycerate
at 29% of the activity with ATP
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?
?
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the enzyme shows highest activity with D-glycerate (100%), and lower activity (34%) with L-glycerate
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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ATP can be partially replaced by GTP, CTP, TTP and UTP (16%, 20%, 16%, and 10% activity, respectively)
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?
additional information
?
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L-glycerate, galactonate, gluconate, malate, pyruvate, lactate, glyceraldehyde, glycerol, serine, 3-phosphoglycerate, ADP, diphosphate, polyphosphate, and glyceraldehyde 3-phosphate are no substrates
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?
additional information
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no activity is observed with ADP, diphosphate and polyphosphates
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additional information
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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
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additional information
?
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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
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additional information
?
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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
-
-
-
additional information
?
-
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
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