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ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
ADP + (R)-glycerate
AMP + 3-phospho-(R)-glycerate
at 32% of the activity with ATP
-
-
?
ADP + D-glycerate
AMP + 2-phospho-D-glycerate
76% activity compared to GTP
-
-
?
AMP + (R)-glycerate
adenosine + 2-phospho-(R)-glycerate
54% of the activity with GTP
-
-
?
AMP + D-glycerate
adenosine + 2-phospho-D-glycerate
54% activity compared to GTP
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
CTP + (R)-glycerate
CDP + 3-phospho-(R)-glycerate
CTP + D-glycerate
CDP + 2-phospho-D-glycerate
87% activity compared to GTP
-
-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
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
-
-
?
GTP + (R)-glycerate
GDP + 2-phospho-(R)-glycerate
GTP + (R)-glycerate
GDP + 3-phospho-(R)-glycerate
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
-
-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
UTP + (R)-glycerate
UDP + 3-phospho-(R)-glycerate
UTP + D-glycerate
UDP + 2-phospho-D-glycerate
81% activity compared to GTP
-
-
?
additional information
?
-
ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
32% of the activity with ATP
-
-
?
ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
76% of the activity with GTP
-
-
?
ADP + (R)-glycerate
AMP + 2-phospho-(R)-glycerate
76% of the activity with GTP
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
enzymes in the (D)-glucarate/galactarate catabolic pathway
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
no activity with (S)-glycerate
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
key enzyme in the Entner-Doudoroff pathway in archaea
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
92% of the activity with GTP
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
key enzyme in the Entner-Doudoroff pathway in archaea
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
92% of the activity with GTP
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 2-phospho-(R)-glycerate
enzyme of the branched Entner-Doudoroff pathway
-
-
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
activity towards L-glycerate is 13% of that towards D-glycerate
2-phosphoglycerate
ir
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
2-phosphoglycerate
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
-
-
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
2-phosphoglycerate
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
-
?
ATP + (R)-glycerate
ADP + 3-phospho-(R)-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-(R)-glycerate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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-D-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
specific substrate
-
-
?
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
-
-
?
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
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
specific substrate
-
-
?
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
-
-
?
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
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
92% activity compared to GTP
-
-
?
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
-
-
?
ATP + D-glycerate
ADP + 2-phospho-D-glycerate
-
-
-
-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
73% of the activity with ATP
-
-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
87% of the activity with GTP
-
-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
87% of the activity with GTP
-
-
?
CTP + (R)-glycerate
CDP + 2-phospho-(R)-glycerate
16% of the activity with ATP
-
-
?
CTP + (R)-glycerate
CDP + 3-phospho-(R)-glycerate
-
at 59% of the activity with ATP
-
-
?
CTP + (R)-glycerate
CDP + 3-phospho-(R)-glycerate
at 73% of the activity with ATP
-
-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
112% of the activity with ATP
-
-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
63% of the activity with ATP
-
-
?
diphosphate + (R)-glycerate
phosphate + 2-phospho-(R)-glycerate
63% of the activity with ATP
-
-
?
GTP + (R)-glycerate
GDP + 2-phospho-(R)-glycerate
64% of the activity with ATP
-
-
?
GTP + (R)-glycerate
GDP + 2-phospho-(R)-glycerate
-
-
-
?
GTP + (R)-glycerate
GDP + 2-phospho-(R)-glycerate
20% of the activity with ATP
-
-
?
GTP + (R)-glycerate
GDP + 3-phospho-(R)-glycerate
-
at 59% of the activity with ATP
-
-
?
GTP + (R)-glycerate
GDP + 3-phospho-(R)-glycerate
at 64% of the activity with ATP
-
-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
29% of the activity with ATP
-
-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
81% of the activity with GTP
-
-
?
UTP + (R)-glycerate
UDP + 2-phospho-(R)-glycerate
10% of the activity with ATP
-
-
?
UTP + (R)-glycerate
UDP + 3-phospho-(R)-glycerate
-
at 64% of the activity with ATP
-
-
?
UTP + (R)-glycerate
UDP + 3-phospho-(R)-glycerate
at 29% of the activity with ATP
-
-
?
additional information
?
-
-
the enzyme shows highest activity with D-glycerate (100%), and lower activity (34%) with L-glycerate
-
-
?
additional information
?
-
-
AMP is not a substrate
-
-
?
additional information
?
-
AMP is not a substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
ATP can be partially replaced by GTP, CTP, TTP and UTP (16%, 20%, 16%, and 10% activity, respectively)
-
-
?
additional information
?
-
-
L-glycerate, galactonate, gluconate, malate, pyruvate, lactate, glyceraldehyde, glycerol, serine, 3-phosphoglycerate, ADP, diphosphate, polyphosphate, and glyceraldehyde 3-phosphate are no substrates
-
-
?
additional information
?
-
no activity is observed with ADP, diphosphate and polyphosphates
-
-
?
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
-
-
-
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
-
-
-
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
-
-
-
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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Sr2+
divalent metal ion required, Sr2+ (10 mM) shows 79% of the activity compared to Mg2+
Zn2+
divalent metal ion required, Zn2+ (10 mM) shows 84% of the activity compared to Mg2+
Ca2+
divalent metal ion required, Ca2+ (10 mM) shows 85% of the activity compared to Mg2+
Ca2+
15% of the activity with Mg2+
Co2+
-
10 mM, 75% of the activity with Mg2+
Co2+
10 mM, 68% of the activity with Mg2+
Co2+
divalent metal ion required, maximal activity in presence of Co2+ or Mg2+ (10 mM)
Co2+
106% activity in the presence of 10 mM Co2+ compared to Mg2+
Co2+
10 mM, can substitute for Mg2+, activity is 8% of the activity activated by Mg2+
Co2+
56% of the activity with Mg2+
K+
-
50 mM, high stimulation
K+
7.94fold increase of activity at 50 mM
K+
50 mM, 7.9fold activation
Li+
2.28fold increase of activity at 50 mM
Li+
50 mM, 2.3fold activation
Mg2+
-
required
Mg2+
-
0.05 mM, most effective divalent cation
Mg2+
10 mM, required for activity
Mg2+
no activity is observed in the absence of divalent metal ion and maximal activity is observed in the presence of Mg2+ (10 mM)
Mg2+
divalent metal ion required, maximal activity in presence of Co2+ or Mg2+ (10 mM)
Mg2+
100% activity in the presence of 10 mM
Mg2+
10 mM, required for activity
Mg2+
-
20 mM, required for highest activity
Mg2+
highest activity is observed in presence of 20 mM Mg2+
Mn2+
-
10 mM, 72% of the activity with 10 mM Mg2+
Mn2+
10 mM, 76% of the activity with Mg2+
Mn2+
divalent metal ion required, Mn2+ (10 mM) shows 93% of the activity compared to Mg2+
Mn2+
10 mM, can substitute for Mg2+, activity is 10% of the activity activated by Mg2+
Mn2+
59% of the activity with Mg2+
Na+
3.49fold increase of activity at 50 mM
Na+
50 mM, 3.5fold activation
NH4+
-
50 mM, high stimulation
NH4+
7.83fold increase of activity at 50 mM
NH4+
50 mM, 7.8fold activation
Ni2+
-
stimulates, 10 mM, 29% of the activity with Mg2+
Ni2+
10 mM, 11% of the activity with Mg2+
Ni2+
divalent metal ion required, Ni2+ (10 mM) shows 68% of the activity compared to Mg2+
Ni2+
30% of the activity with Mg2+
additional information
-
Mg2+ can be replaced to some extent by Ni2+ (25%), Mn2+ (11%), and Co2+ (11%)
additional information
-
no activating effect of K+
additional information
-
when Mn2+, Co2+, Ca2+, Sr2+ and Ni2+ is substituted for Mg2+, respectively, Mn2+, Co2+ and Ni2+ show 76, 68 and 11% activity of that for Mg2+
additional information
when Mn2+, Co2+, Ca2+, Sr2+ and Ni2+ is substituted for Mg2+, respectively, Mn2+, Co2+ and Ni2+ show 76, 68 and 11% activity of that for Mg2+
additional information
monovalent metal ions have no effect on the enzyme activity
additional information
-
when divalent metal ions, such as Mn2+, Co2+, Ni2+, Zn2+, Ca2+, and Sr2+, are substituted for Mg2+, the enzyme activity is less than 10% of that obtained in the presence of Mg2+
additional information
when divalent metal ions, such as Mn2+, Co2+, Ni2+, Zn2+, Ca2+, and Sr2+, are substituted for Mg2+, the enzyme activity is less than 10% of that obtained in the presence of Mg2+
additional information
-
Co2+, Mn2+, and Ni2+ (all 5 mM), and Ca2+ (2 mM) can partially replace Mg2+ (56%, 59%, 30% and 15% activity, respectively)
additional information
-
K+ and NH4+ do not stimulate activity
additional information
-
no activity is detected in the presence of Cu2+ and Fe2+ at 0.2, 2, 5 and 20 mM
additional information
no activity is detected in the presence of Cu2+ and Fe2+ at 0.2, 2, 5 and 20 mM, respectively
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Hubbard, B.K.; Koch, M.; Palmer, D.R.J.; Babbitt, P.C.; Gerlt, J.A.
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli
Biochemistry
37
14369-14375
1998
Escherichia coli
brenda
Hill, B.; Attwood, M.M.
The purification of glycerate kinase from Hyphomicrobium sp. and Pseudomonas AM1: product identification
J. Gen. Microbiol.
83
187-190
1974
Hyphomicrobium sp., Pseudomonas sp.
brenda
Yoshida, T.; Fukuta, K.; Mitsunaga, T.; Yamada, H.; Izumi, Y.
Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2
Eur. J. Biochem.
210
849-854
1992
Hyphomicrobium methylovorum
brenda
Noh, M.; Jung, J.H.; Lee, S.B.
Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family
Biotechnol. Bioprocess Eng.
11
344-350
2006
Saccharolobus solfataricus, Saccharolobus solfataricus P2, Thermoplasma acidophilum, Thermoplasma acidophilum (Q9HKZ0)
-
brenda
Kehrer, D.; Ahmed, H.; Brinkmann, H.; Siebers, B.
Glycerate kinase of the hyperthermophilic archaeon Thermoproteus tenax: new insights into the phylogenetic distribution and physiological role of members of the three different glycerate kinase classes
BMC Genet.
8
301
2007
Thermoproteus tenax
brenda
Liu, B.; Hong, Y.; Wu, L.; Li, Z.; Ni, J.; Sheng, D.; Shen, Y.
A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization
Extremophiles
11
733-739
2007
Pyrococcus horikoshii, Pyrococcus horikoshii (O58231)
brenda
Reher, M.; Bott, M.; Schoenheit, P.
Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus
FEMS Microbiol. Lett.
259
113-119
2006
Picrophilus torridus
brenda
Kehrer, D.; Ahmed, H.; Brinkmann, H.; Siebers, B.
Glycerate kinase of the hyperthermophilic archaeon Thermoproteus tenax: new insights into the phylogenetic distribution and physiological role of members of the three different glycerate kinase classes
BMC Genomics
8
301
2007
Thermoproteus tenax (Q703V9)
brenda
Bartsch, O.; Hagemann, M.; Bauwe, H.
Only plant-type (GLYK) glycerate kinases produce d-glycerate 3-phosphate
FEBS Lett.
582
3025-3028
2008
Escherichia coli K-12 (P23524), Escherichia coli K-12 (P77364), Synechocystis sp. (P73408)
brenda
Liu, B.; Wu, L.; Liu, T.; Hong, Y.; Shen, Y.; Ni, J.
A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties
Biotechnol. Lett.
31
1937-1941
2009
Sulfurisphaera tokodaii (Q96YZ3), Sulfurisphaera tokodaii 7 (Q96YZ3)
brenda
Sims, P.A
Reed, G.H.: Method for the enzymatic synthesis of 2-phospho-D-glycerate from adenosine 5'-triphosphate and D-glycerate via D-glycerate-2-kinase
J. Mol. Catal. B
32
77-81
2005
Escherichia coli
-
brenda
Kouril, T.; Wieloch, P.; Reimann, J.; Wagner, M.; Zaparty, M.; Albers, S.V.; Schomburg, D.; Ruoff, P.; Siebers, B.
Unraveling the function of the two Entner-Doudoroff branches in the thermoacidophilic crenarchaeon Sulfolobus solfataricus P2
FEBS J.
280
1126-1138
2013
Saccharolobus solfataricus (Q7LXP1), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q7LXP1), Saccharolobus solfataricus P2
brenda
Sass, J.O.; Fischer, K.; Wang, R.; Christensen, E.; Scholl-Buergi, S.; Chang, R.; Kapelari, K.; Walter, M.
D-glyceric aciduria is caused by genetic deficiency of D-glycerate kinase (GLYCTK)
Hum. Mutat.
31
1280-1285
2010
Homo sapiens
brenda
Keech, O.; Gardeström, P.; Kleczkowski, L.; Rouhier, N.
The redox control of photorespiration: From biochemical and physiological aspects to biotechnological considerations
Plant Cell Environ.
40
553-569
2017
Arabidopsis thaliana, Zea mays
brenda
Zelcbuch, L.; Razo-Mejia, M.; Herz, E.; Yahav, S.; Antonovsky, N.; Kroytoro, H.; Milo, R.; Bar-Even, A.
An in vivo metabolic approach for deciphering the product specificity of glycerate kinase proves that both E. colis glycerate kinases generate 2-phosphoglycerate
PLoS ONE
10
e0122957
2015
Escherichia coli
brenda
Schwarzenbacher, R.; McMullan, D.; Krishna, S.; Xu, Q.; Miller, M.; Canaves, J.; Elsliger, M.; Floyd, R.; Grzechnik, S.; Jaroszewski, L.; Klock, H.; Koesema, E.; Kovarik, J.; Kreusch, A.; Kuhn, P.; McPhillips, T.; Morse, A.; Quijano, K.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima at 2.70 A resolution reveals a new fold
Proteins
65
243-248
2006
Thermotoga maritima (Q9X1S1), Thermotoga maritima DSM 3109 (Q9X1S1)
brenda
Hardt, N.; Kinfu, B.M.; Chow, J.; Schoenenberger, B.; Streit, W.R.; Obkircher, M.; Wohlgemuth, R.
Biocatalytic asymmetric phosphorylation catalyzed by recombinant glycerate-2-kinase
ChemBioChem
18
1518-1522
2017
Thermotoga maritima (Q9X1S1), Thermotoga maritima DSM 3109 (Q9X1S1), Thermotoga maritima ATCC 43589 (Q9X1S1), Thermotoga maritima JCM 10099 (Q9X1S1)
brenda
Fox, K.; Prather, K.
Production of d-Glyceric acid from d-Galacturonate in Escherichia coli
J. Ind. Microbiol. Biotechnol.
47
1075-1081
2020
Escherichia coli (P23524)
brenda