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Literature summary for 2.7.1.165 extracted from

  • 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 (2017), ChemBioChem, 18, 1518-1522 .
    View publication on PubMed
Search for more literature for 2.7.1.165

Application

Application Comment Organism
synthesis straightforward phosphorylation reaction by enzyme GCK and subsequent product isolation enables the preparation of enantiomerically pure D-glycerate 2-phosphate. This phosphorylation reaction, using recombinant glycerate-2-kinase, yields D-glycerate 2-phosphate in fewer reaction steps and with higher purity than chemical routes Thermotoga maritima

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the enzyme as maltose-binding protein fusion in Escherichia coli strain BL21(DE3) Thermotoga maritima

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Thermotoga maritima
0.13
-
 D-glycerate recombinant enzyme, pH 7.0, 37°C Thermotoga maritima

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-glycerate Thermotoga maritima
-
 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate Thermotoga maritima DSM 3109
-
 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate Thermotoga maritima ATCC 43589
-
 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate Thermotoga maritima JCM 10099
-
 ADP + 2-phospho-(R)-glycerate
-
 ?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X1S1
-
-
Thermotoga maritima ATCC 43589 Q9X1S1
-
-
Thermotoga maritima DSM 3109 Q9X1S1
-
-
Thermotoga maritima JCM 10099 Q9X1S1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding protein fusion enzyme from Escherichia coli strain BL21(DE3) by amylose affinity chromatography and cleavage of the MBP-tag Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-glycerate
-
 Thermotoga maritima ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid Thermotoga maritima ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate
-
 Thermotoga maritima DSM 3109 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid Thermotoga maritima DSM 3109 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate
-
 Thermotoga maritima ATCC 43589 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid Thermotoga maritima ATCC 43589 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate
-
 Thermotoga maritima JCM 10099 ADP + 2-phospho-(R)-glycerate
-
 ?
ATP + D-glycerate the enzyme shows selectivity and excellent enantioselectivity towards phosphorylation of the D-enantiomer of glyceric acid Thermotoga maritima JCM 10099 ADP + 2-phospho-(R)-glycerate
-
 ?
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 Thermotoga maritima ?
-
-
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 Thermotoga maritima DSM 3109 ?
-
-
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 Thermotoga maritima ATCC 43589 ?
-
-
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 Thermotoga maritima JCM 10099 ?
-
-

Subunits

Subunits Comment Organism
? x * 87000, recombinant MBP-tagged enzyme, SDS-PAGE, x * 52000, recombinant detagged enzyme, SDS-PAGE Thermotoga maritima

Synonyms

Synonyms Comment Organism
D-glycerate 2-kinase
-
 Thermotoga maritima
GCK
-
 Thermotoga maritima
TM1585
-
 Thermotoga maritima
TM_1585 locus name Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
 recombinant enzyme Thermotoga maritima

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 90 the temperature dependence of the specific activity shows a large increase from 37°C to 80°C, plateauing at 90°C Thermotoga maritima

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.054
-
 D-glycerate recombinant enzyme, pH 7.0, 37°C Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.2
-
 recombinant enzyme Thermotoga maritima

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.415
-
 D-glycerate recombinant enzyme, pH 7.0, 37°C Thermotoga maritima