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ADP + sn-glycerol 3-phosphate
ATP + glycerol
ATP + 1,3-propanediol
ADP + ?
Candida mycoderma
-
weak
-
-
?
ATP + 1-deoxy-sn-glycerol
ADP + ?
Candida mycoderma
-
-
-
-
?
ATP + 2-deoxyglycerol
ADP + ?
Candida mycoderma
-
-
-
-
?
ATP + 2-mercaptoethanol
ADP + ?
Candida mycoderma
-
-
-
-
?
ATP + 2-methylglycerol
ADP + ?
Candida mycoderma
-
-
-
-
?
ATP + aminopropanediol
ADP + ?
Candida mycoderma
-
R- and S-
-
-
?
ATP + D-glyceraldehyde
ADP + D-glyceraldehyde 3-phosphate
-
-
-
-
?
ATP + dichloro-monoacetin
?
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
ATP + dihydroxypropyl dichloroacetate
ADP + ?
-
glycerol analogue
-
-
?
ATP + glyceric acid
ADP + ?
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
ATP + L-glyceraldehyde
ADP + L-glyceraldehyde 3-phosphate
ATP + mercaptopropanediol
1-mercaptopropanediol 1-phosphate + ADP
ATP + monoacetin
ADP + ?
-
glycerol analogue
-
-
?
ATP + monobutyrin
ADP + ?
-
glycerol analogue
-
-
?
ATP + monothioglycerol
ADP + ?
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
glycerol + ATP
sn-glycerol 3-phosphate + ADP
GTP + glycerol
GDP + glycerol 3-phosphate
ITP + glycerol
IDP + glycerol 3-phosphate
TTP + glycerol
TDP + glycerol 3-phosphate
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
XTP + glycerol
XDP + glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
additional information
?
-
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ADP + sn-glycerol 3-phosphate
ATP + glycerol
-
-
-
r
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
Candida mycoderma
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + glyceric acid
?
Candida mycoderma
-
-
-
-
?
ATP + glyceric acid
?
-
-
-
-
?
ATP + glycerol
?
-
-
-
-
?
ATP + glycerol
?
-
enzyme functions primarily in the utilization of glycerol as a carbon and energy source
-
-
?
ATP + glycerol
?
-
dissimilation of glycerol
-
-
?
ATP + glycerol
?
-
higher organisms: salvage of glycerol released upon lipolysis
-
-
?
ATP + glycerol
?
-
key enzyme for glycerol use in phospholipid synthesis
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
Candida mycoderma
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
Candida mycoderma
-
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
Candida mycoderma
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
only glycerol active as phosphoryl group acceptor
-
-
ir
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
641297, 641298, 641300, 641303, 641309, 641311, 641317, 641320, 661122, 701908, 722712 -
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
high specificity for ATP, no other ribonucleoside triphosphate utilized
-
-
ir
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
high specificity for ATP, no other ribonucleoside triphosphate utilized
i.e. L-alpha-glycerophosphate
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
key enzyme of glycerol metabolism in bacteria, phosphorylation of glycerol prevents diffusion through membrane
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
enzyme deficiency causes hyperglycerolemia and glyceroluria
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme deficiency causes hyperglycerolemia and glyceroluria, provides glycerol 3-phosphate which is an important intermediate between glucose and lipid metabolism
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
involved in fat and carbohydrate metabolism, glycerol 3-phosphate is important for the synthesis of glycerides, glycerol lipids and dihydroxyacetone phosphate
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
involved in fat and carbohydrate metabolism, glycerol 3-phosphate is important for the synthesis of glycerides, glycerol lipids and dihydroxyacetone phosphate
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
Mycobacterium butyricum
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
weak: GTP, CTP, UTP, ITP
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
trout
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
CTP or UTP are as effective as ATP, not: GTP
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
r
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
enzyme can utilize only ATP as phosphoryl group donor
-
-
?
ATP + glycerol
ADP + sn-glycerol 3-phosphate
-
-
-
-
?
ATP + L-glyceraldehyde
ADP + L-glyceraldehyde 3-phosphate
Candida mycoderma
-
-
-
-
?
ATP + L-glyceraldehyde
ADP + L-glyceraldehyde 3-phosphate
-
-
-
-
?
ATP + L-glyceraldehyde
ADP + L-glyceraldehyde 3-phosphate
-
-
-
-
?
ATP + mercaptopropanediol
1-mercaptopropanediol 1-phosphate + ADP
Candida mycoderma
-
-
-
?
ATP + mercaptopropanediol
1-mercaptopropanediol 1-phosphate + ADP
Candida mycoderma
-
-
-
-
?
ATP + mercaptopropanediol
1-mercaptopropanediol 1-phosphate + ADP
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
-
14% of the activity with ATP
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
-
-
-
-
?
CTP + glycerol
CDP + glycerol 3-phosphate
-
-
-
-
?
glycerol + ATP
sn-glycerol 3-phosphate + ADP
-
-
-
?
glycerol + ATP
sn-glycerol 3-phosphate + ADP
-
-
-
-
?
glycerol + ATP
sn-glycerol 3-phosphate + ADP
-
-
-
-
?
glycerol + ATP
sn-glycerol 3-phosphate + ADP
-
-
-
?
GTP + glycerol
GDP + glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
GTP + glycerol
GDP + glycerol 3-phosphate
-
-
-
-
?
GTP + glycerol
GDP + glycerol 3-phosphate
-
-
-
-
?
GTP + glycerol
GDP + glycerol 3-phosphate
-
-
-
-
?
ITP + glycerol
IDP + glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
ITP + glycerol
IDP + glycerol 3-phosphate
-
-
-
-
?
ITP + glycerol
IDP + glycerol 3-phosphate
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
Candida mycoderma
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
-
7% of the activity with ATP
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
-
-
-
-
?
UTP + glycerol
UDP + glycerol 3-phosphate
-
-
-
-
?
additional information
?
-
Candida mycoderma
-
-
-
-
?
additional information
?
-
Candida mycoderma
-
D-glyceraldehyde promotes conversion of ATP to ADP + phosphate
-
-
?
additional information
?
-
Candida mycoderma
-
overview: enzyme catalyzes the phosphorylation of 28 nitrogen-, sulfur- and alkyl-substituted analogues of glycerol, phosphorylated products have stereochemistry analogous to that of sn-glycerol 3-phosphate
-
-
?
additional information
?
-
-
combined assay of lipase, glycerol kinase, and glycerol-3-phosphate oxidase immobilized onto nanoparticles aggregates as part of a biosensot electrode (onto nanocomposite of ZnONPs/chitosan electrodeposited onto Pt electrode)
-
-
-
additional information
?
-
-
the enzyme exhibits two-step kinetics as a function of ATP at a fixed Mg2+ concentration due to the formation of multiple Mg-ATP complexes at different Mg2+ to ATP molar ratio. The interaction of Mg2+ and ATP generates Mg-ATP complexes of various physical and chemical features in which the product composition depends on Mg2+ to ATP molar ratio among other factors such as pH, temperature, availability of other polyvalent chelating anions, as well as cations and their concentration. The Ca2+ salt of ATP is not an appropriate substrate for glycerol kinase
-
-
-
additional information
?
-
-
D-glyceraldehyde promotes conversion of ATP to ADP + phosphate
-
-
?
additional information
?
-
-
overview: enzyme catalyzes the phosphorylation of 28 nitrogen-, sulfur- and alkyl-substituted analogues of glycerol, phosphorylated products have stereochemistry analogous to that of sn-glycerol 3-phosphate
-
-
?
additional information
?
-
-
phosphate rather than D-glyceraldehyde 3-phosphate is formed, the hydrated form of this triose is phosphorylated in position 1 to yield an unstable intermediate that decomposes to D-glyceraldehyde + phosphate
-
-
?
additional information
?
-
-
overview: enzyme catalyzes the phosphorylation of 28 nitrogen-, sulfur- and alkyl-substituted analogues of glycerol, phosphorylated products have stereochemistry analogous to that of sn-glycerol 3-phosphate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
overview: enzyme catalyzes the phosphorylation of 28 nitrogen-, sulfur- and alkyl-substituted analogues of glycerol, phosphorylated products have stereochemistry analogous to that of sn-glycerol 3-phosphate
-
-
?
additional information
?
-
hexameric glycerol kinase (GK) from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (Tk-GK) is identified as the substrate-binding form of the enzyme
-
-
-
additional information
?
-
-
hexameric glycerol kinase (GK) from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (Tk-GK) is identified as the substrate-binding form of the enzyme
-
-
-
additional information
?
-
hexameric glycerol kinase (GK) from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (Tk-GK) is identified as the substrate-binding form of the enzyme
-
-
-
additional information
?
-
hexameric glycerol kinase (GK) from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (Tk-GK) is identified as the substrate-binding form of the enzyme
-
-
-
additional information
?
-
in addition to its widely known and expected phosphotransferase (class II) activity, TbgGK can efficiently facilitate the hydrolytic cleavage of phosphoric anhydride bonds (a class III property). 4-Nitrophenylphosphate (pNPP) dephosphorylation is TbgGK-mediated, LC-MS analysis of the TbgGK-catalyzed dephosphorylation of its physiological substrate
-
-
-
additional information
?
-
-
in addition to its widely known and expected phosphotransferase (class II) activity, TbgGK can efficiently facilitate the hydrolytic cleavage of phosphoric anhydride bonds (a class III property). 4-Nitrophenylphosphate (pNPP) dephosphorylation is TbgGK-mediated, LC-MS analysis of the TbgGK-catalyzed dephosphorylation of its physiological substrate
-
-
-
additional information
?
-
in addition to its widely known and expected phosphotransferase (class II) activity, TbgGK can efficiently facilitate the hydrolytic cleavage of phosphoric anhydride bonds (a class III property). 4-Nitrophenylphosphate (pNPP) dephosphorylation is TbgGK-mediated, LC-MS analysis of the TbgGK-catalyzed dephosphorylation of its physiological substrate
-
-
-
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
although there are two African human pathogenic Trypanosoma subspecies: Trypanosoma brucei gambiense (Tbg) and Trypanosoma brucei rhodesiense (Tbr), it is reported in that the amino acid sequences of their GKs are exactly identical. Hence, TbgGK represents the glycerol kinase of both subspecies
evolution
although there are two African human pathogenic Trypanosoma subspecies: Trypanosoma brucei gambiense (Tbg) and Trypanosoma brucei rhodesiense (Tbr), it is reported in that the amino acid sequences of their GKs are exactly identical. Hence, TbgGK represents the glycerol kinase of both subspecies
evolution
Bacteria and Eukarya have cell membranes with sn-glycerol-3-phosphate (G3P), whereas archaeal membranes contain sn-glycerol-1-phosphate (G1P). Determining the time at which cells with either G3P-lipid membranes or G1P-lipid membranes appeared is important for understanding the early evolution of terrestrial life. Reconstructed molecular phylogenetic trees of G1PDH (G1P dehydrogenase, EgsA/AraM), which is responsible for G1P synthesis and G3PDHs (G3P dehydrogenase, GpsA and GlpA/GlpD), and glycerol kinase (GlpK), which is responsible for G3P synthesis. Together with the distribution of these protein-encoding genes among archaeal and bacterial groups, phylogenetic analyses suggest that GlpA/GlpD in the Commonote (the last universal common ancestor of all extant life with a cellular form, Commonote commonote) acquired EgsA (G1PDH) from the archaeal common ancestor (Commonote archaea) and acquired GpsA and GlpK from a bacterial common ancestor (Commonote bacteria). The Commonote probably possessed a G3P-lipid membrane synthesized enzymatically, after which the archaeal lineage acquires G1PDH followed by the replacement of a G3P-lipid membrane with a G1P-lipid membrane. Detailed overview
evolution
both Gykl1 and Gk2 are thought to have arisen by the transposition of Gk located on the X chromosome, and have high homology with Gk. But both Gykl1 and Gk2 show testis-specific expression, and the proteins have no glycerol kinase activity in vitro, unlike GK and GK5
evolution
glycerol kinase is a member of the ATPase superfamily, which includes hexokinase, actin, and heat shock protein. These share a common betabetabetaalphabetaalphabetaalpha folding motif and markedly change conformation upon substrate binding because of interdomain motion
evolution
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glycerol kinase is a member of the ATPase superfamily, which includes hexokinase, actin, and heat shock protein. These share a common betabetabetaalphabetaalphabetaalpha folding motif and markedly change conformation upon substrate binding because of interdomain motion
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evolution
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glycerol kinase is a member of the ATPase superfamily, which includes hexokinase, actin, and heat shock protein. These share a common betabetabetaalphabetaalphabetaalpha folding motif and markedly change conformation upon substrate binding because of interdomain motion
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malfunction
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a glycerol kinase knockout strain is incapable to grow on glycerol and shows higher NADPH-dependent xylitol production compared to the wild type strain
malfunction
frequently observed variation in the glpK coding sequence produces a drug-tolerant phenotype that can reduce antibiotic efficacy and may contribute to the evolution of resistance. Common variation in a homopolymeric region in the glpK gene is associated with drug resistance in clinical isolates. Glycerol catabolic defects are associated with extensive drug resistance in Korea. A panel of Korean Mycobacterium tuberculosis isolates that vary in drug sensitivity profiles, from fully sensitive strains to extensively evolved clones that are phenotypically resistant to more than ten different antibiotics. GlpK frameshift mutations are common in Mycobacterium tuberculosis isolates and associated with drug resistance in Peru
malfunction
Gk2-deficient mice show male infertility with disordered mitochondrial sheath formation. Gk2 disrupted mice are male infertile because their spermatozoa cannot pass through the uterotubal junction (UTJ) due to reduced motility. Disorganization of the mitochondrial sheath occurs in glycerol kinase 2 (Gk2) disrupted mice
malfunction
overexpression of glycerol kinase GlcA bypasses the requirement of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), encoded by gene gfdA, in glucose media for colony growth. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media
malfunction
overexpression of glycerol kinase under oxidative stress with glycerol supplementation leads to enhancement of lipid production in Synechocystis sp. PCC 6803
malfunction
silencing GK5 in PC9R cells induces mitochondrial damage, caspase activation, cell cycle arrest, and apoptosis via SREBP1/SCD1 signaling pathway. The exosomal mRNA of GK5 in the plasma of patients with gefitinib-resistant adenocarcinoma is significantly higher compared with that of gefitinib-sensitive patients. GK5 knockdown induces PC9R cell apoptosis and cell cycle arrest in the presence of gefitinib, as well as PC9R cell mitochondrial dysfunction and caspase activation. GK5 knockdown suppresses tumor proliferation in vivo
malfunction
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overexpression of glycerol kinase GlcA bypasses the requirement of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), encoded by gene gfdA, in glucose media for colony growth. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media
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malfunction
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a glycerol kinase knockout strain is incapable to grow on glycerol and shows higher NADPH-dependent xylitol production compared to the wild type strain
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malfunction
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overexpression of glycerol kinase GlcA bypasses the requirement of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), encoded by gene gfdA, in glucose media for colony growth. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media
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malfunction
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frequently observed variation in the glpK coding sequence produces a drug-tolerant phenotype that can reduce antibiotic efficacy and may contribute to the evolution of resistance. Common variation in a homopolymeric region in the glpK gene is associated with drug resistance in clinical isolates. Glycerol catabolic defects are associated with extensive drug resistance in Korea. A panel of Korean Mycobacterium tuberculosis isolates that vary in drug sensitivity profiles, from fully sensitive strains to extensively evolved clones that are phenotypically resistant to more than ten different antibiotics. GlpK frameshift mutations are common in Mycobacterium tuberculosis isolates and associated with drug resistance in Peru
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malfunction
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overexpression of glycerol kinase GlcA bypasses the requirement of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), encoded by gene gfdA, in glucose media for colony growth. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media
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metabolism
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the enzyme plays an essential role in central and lipid metabolism
metabolism
an EIIA homologue in the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS or KPN00353, UniProt ID A6T5D4), negatively regulates the 1,3-propanediol (1,3-PD) production in Klebsiella pneumoniae, mutational analysis, overview. Residue His65 of KPN00353 is important for binding to GlpK, weak binding to enzyme GlpK mutant H65Q
metabolism
glycerol 3-phosphate (G3P) can be synthesized by two classical pathways. The first pathway is catalyzed by an NAD-dependent glycerol 3-phosphate dehydrogenase converting dihydroxyacetone phosphate (DHAP) into G3P The second pathway is catalyzed by a glycerol kinase encoded by glcA converting glycerol to G3P
metabolism
glycerol kinase (GK) is a key enzyme of glycerol metabolism. It participates in glycolysis and lipid membrane biosynthesis
metabolism
glycerol kinase interacts with nuclear receptor NR4A1 and regulates glucose metabolism in the liver, Gyk interacts with NR4A1 in the nucleus
metabolism
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lipase, glycerol kinase, and glycerol-3-phosphate oxidase are required for lipid analysis in a cascade reaction
metabolism
Mycobacterium tuberculosis genes that alter the rate of bacterial clearance in drug-treated mice. Several functionally distinct bacterial genes are found to alter bacterial clearance, and prominent among these is the glpK gene that encodes the glycerol-3-kinase enzyme that is necessary for glycerol catabolism. Growth on glycerol generally increases the sensitivity of Mycobacterium tuberculosis to antibiotics in vitro, and glpK-deficient bacteria persist during antibiotic treatment in vivo, particularly during exposure to pyrazinamide-containing regimens. Reversible high-frequency variation in carbon metabolic pathways can produce phenotypically drug-tolerant clones and have a role in the development of resistance. The glycerol metabolism increases drug efficacy in vitro and during murine infection, overview
metabolism
overview of the stereospecific biosynthetic pathways of glycerol 1-phosphate (G1P) and glycerol 3-phosphate (G3P)
metabolism
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an EIIA homologue in the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS or KPN00353, UniProt ID A6T5D4), negatively regulates the 1,3-propanediol (1,3-PD) production in Klebsiella pneumoniae, mutational analysis, overview. Residue His65 of KPN00353 is important for binding to GlpK, weak binding to enzyme GlpK mutant H65Q
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metabolism
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glycerol kinase (GK) is a key enzyme of glycerol metabolism. It participates in glycolysis and lipid membrane biosynthesis
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metabolism
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glycerol 3-phosphate (G3P) can be synthesized by two classical pathways. The first pathway is catalyzed by an NAD-dependent glycerol 3-phosphate dehydrogenase converting dihydroxyacetone phosphate (DHAP) into G3P The second pathway is catalyzed by a glycerol kinase encoded by glcA converting glycerol to G3P
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metabolism
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an EIIA homologue in the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS or KPN00353, UniProt ID A6T5D4), negatively regulates the 1,3-propanediol (1,3-PD) production in Klebsiella pneumoniae, mutational analysis, overview. Residue His65 of KPN00353 is important for binding to GlpK, weak binding to enzyme GlpK mutant H65Q
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metabolism
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glycerol 3-phosphate (G3P) can be synthesized by two classical pathways. The first pathway is catalyzed by an NAD-dependent glycerol 3-phosphate dehydrogenase converting dihydroxyacetone phosphate (DHAP) into G3P The second pathway is catalyzed by a glycerol kinase encoded by glcA converting glycerol to G3P
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metabolism
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Mycobacterium tuberculosis genes that alter the rate of bacterial clearance in drug-treated mice. Several functionally distinct bacterial genes are found to alter bacterial clearance, and prominent among these is the glpK gene that encodes the glycerol-3-kinase enzyme that is necessary for glycerol catabolism. Growth on glycerol generally increases the sensitivity of Mycobacterium tuberculosis to antibiotics in vitro, and glpK-deficient bacteria persist during antibiotic treatment in vivo, particularly during exposure to pyrazinamide-containing regimens. Reversible high-frequency variation in carbon metabolic pathways can produce phenotypically drug-tolerant clones and have a role in the development of resistance. The glycerol metabolism increases drug efficacy in vitro and during murine infection, overview
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metabolism
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glycerol kinase (GK) is a key enzyme of glycerol metabolism. It participates in glycolysis and lipid membrane biosynthesis
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metabolism
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glycerol 3-phosphate (G3P) can be synthesized by two classical pathways. The first pathway is catalyzed by an NAD-dependent glycerol 3-phosphate dehydrogenase converting dihydroxyacetone phosphate (DHAP) into G3P The second pathway is catalyzed by a glycerol kinase encoded by glcA converting glycerol to G3P
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physiological function
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glycerol kinase expression leads to increased fat storage in H4IIE rat hepatoma cells
physiological function
the enzyme is essential for energy metabolism
physiological function
enzyme glycerol kinase 2 (GK2) is essential for proper arrangement of crescent-like mitochondria to form the mitochondrial sheath during mouse spermatogenesis
physiological function
GK5 confers gefitinib resistance in lung cancer by inhibiting apoptosis and cell cycle arrest. Role of glycerol kinase 5 (GK5) in mediating gefitinib resistance in non-small cell lung cancer (NSCLC), overview. GK5 confers gefitinib resistance through upregulating SCD1 expression, molecular mechanism underlying GK5-mediated gefitinib resistance
physiological function
glycerol kinase (GK) catalyzes the Mg/ATP-dependent phosphorylation of glycerol to produce glycerol-3-phosphate which is an important metabolic intermediate in glycolysis. In the absence of glycerol, Tk-GK was a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of enzyme Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
physiological function
glycerol kinase (GlpK) is responsible for sn-glycerol 3-phosphate (G3P) synthesis
physiological function
glycerol kinase (Gyk), consisting of 4 isoforms, plays a critical role in metabolism by converting glycerol to glycerol 3-phosphate in an ATP-dependent reaction. The nuclear orphan receptor subfamily 4 group A member (NR4A)-1 (also known as Nur77, NGFI-B, NAK-1, or TR3is) an important regulator of hepatic glucose homeostasis and lipid metabolism in adipose tissue. Nuclear Gyk isoform b is a corepressor of NR4A1 in the liver. This recruitment is dependent on the C-terminal ligand-binding domain instead of the N-terminal activation function 1 domain, which interacts with other NR4A1 coregulators. NR4A1 transcriptional activity is inhibited by Gyk via protein-protein interaction but not enzymatic activity. Moreover, Gyk overexpression suppresses NR4A1 ability to regulate the expression of target genes involved in hepatic gluconeogenesis in vitro and in vivo as well as blood glucose regulation, which is observed in both unfed and diabetic transfected mice. Moonlighting function of nuclear Gyk isozyme b, which acts as a coregulator of NR4A1, participating in the regulation of hepatic glucose homeostasis in the unfed state and diabetes. The Gyk activity does not affect the interaction between Gyk and NR4A1, Gyk antagonizes the effects of NR4A1 on hepatic gluconeogenesis in vitro and in vivo
physiological function
glycerol plays an important role in the adaptation of fungi to various microenvironments and stressors, including heat shock, anoxic conditions and osmotic stress. Glycerol kinase GlcA coordinately adapts to various carbon sources and osmotic stress in Aspergillus fumigatus. It is suggested that glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source, functional relationship between gfdA and glcA, overview
physiological function
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the enzyme is essential for energy metabolism
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physiological function
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glycerol kinase (GK) catalyzes the Mg/ATP-dependent phosphorylation of glycerol to produce glycerol-3-phosphate which is an important metabolic intermediate in glycolysis. In the absence of glycerol, Tk-GK was a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of enzyme Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
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physiological function
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glycerol plays an important role in the adaptation of fungi to various microenvironments and stressors, including heat shock, anoxic conditions and osmotic stress. Glycerol kinase GlcA coordinately adapts to various carbon sources and osmotic stress in Aspergillus fumigatus. It is suggested that glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source, functional relationship between gfdA and glcA, overview
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physiological function
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glycerol plays an important role in the adaptation of fungi to various microenvironments and stressors, including heat shock, anoxic conditions and osmotic stress. Glycerol kinase GlcA coordinately adapts to various carbon sources and osmotic stress in Aspergillus fumigatus. It is suggested that glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source, functional relationship between gfdA and glcA, overview
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physiological function
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glycerol kinase (GK) catalyzes the Mg/ATP-dependent phosphorylation of glycerol to produce glycerol-3-phosphate which is an important metabolic intermediate in glycolysis. In the absence of glycerol, Tk-GK was a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of enzyme Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol
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physiological function
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glycerol plays an important role in the adaptation of fungi to various microenvironments and stressors, including heat shock, anoxic conditions and osmotic stress. Glycerol kinase GlcA coordinately adapts to various carbon sources and osmotic stress in Aspergillus fumigatus. It is suggested that glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source, functional relationship between gfdA and glcA, overview
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additional information
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detailed kinetic analysis of glycerol kinase as a function of Mg2+ to ATP molar ratio, and multinuclear NMR study of the Mg-ATP complex formation is described in order to elucidate the effect of Mg2+ in modifying the physical and chemical features of ATP, and mechanistic elucidation of the effect of Mg-ATP interaction on the catalytic properties of glycerol kinase, overview
additional information
NR4A1-Gyk b interaction analysis using protein fragments
additional information
the enzyme uses a common catalytic site for both activities, phosphatase and kinase
additional information
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the enzyme uses a common catalytic site for both activities, phosphatase and kinase
additional information
the enzyme uses a common catalytic site for both activities, phosphatase and kinase
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A344V
the mutant shows a higher melting temperature than the wild type enzyme
A344V/T386I/F388Y
the mutant with decreased catalytic efficiency shows a higher melting temperature than the wild type enzyme
C292A
the mutant shows a lower melting temperature than the wild type enzyme
L274M
the mutant shows a higher melting temperature than the wild type enzyme
L274M/T386I/F388Y
the mutant shows a higher melting temperature than the wild type enzyme
Q50E/T386I/F388Y
the mutant shows a higher melting temperature than the wild type enzyme
T386I
the mutant shows a higher melting temperature than the wild type enzyme
T386I/F388Y
the mutant with decreased catalytic efficiency shows a 9°C higher melting temperature than the wild type enzyme
A344V
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the mutant shows a higher melting temperature than the wild type enzyme
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C292A
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the mutant shows a lower melting temperature than the wild type enzyme
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L274M
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the mutant shows a higher melting temperature than the wild type enzyme
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T386I
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the mutant shows a higher melting temperature than the wild type enzyme
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T386I/F388Y
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the mutant with decreased catalytic efficiency shows a 9°C higher melting temperature than the wild type enzyme
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S414N
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increased thermostability, mechanism of stabilization
H232E
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residue located in the activation loop
H232R
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residue located in the activation loop, mutant protein has enhanced activity
D72V
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the catalytic properties of the mutant differ little from those of the wild type enzyme. The mutant shows 14.76% expression compared to the wild type enzyme
E121C
mutant protein is labeled with extrinsic fluorophores for FRET
E478C
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mutation increases the affinity for glucose-specific phosphocarrier protein of the phosphoenolpyruvate:glucose phosphotransferase system (IIA(Glc))
E478C/T428V/R429N
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T428V and R429N replace two coupling locus amino acids with those from Haemophilus influenzae glycerol kinase
E92C
mutant protein is labeled with extrinsic fluorophores for FRET
G304S
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no inhibition by allosteric ligands, mechanism
G427D/T428V/R429N
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replacement of all three of the coupling locus amino acids with those from Haemophilus influenzae glycerol kinase
I474A
the maximum extent of IIAGlc inhibition is reduced for the mutant enzyme
I474C
the maximum extent of IIAGlc inhibition is reduced for the mutant enzyme
I474D
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crystal structure
M271I
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the mutant shows strongly increased Km for ATP and 30.75% expression compared to the wild type enzyme
Q37P
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the mutant shows strongly increased Km for ATP and 65.73% expression compared to the wild type enzyme
R369A
oligomeric interactions are disturbed by the amino acid substitution
R479A
the maximum extent of IIAGlc inhibition is reduced for the mutant enzyme
R479C
the maximum extent of IIAGlc inhibition is reduced for the mutant enzyme
V61L
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the catalytic properties of the mutant differ little from those of the wild type enzyme. The mutant shows 12.71% expression compared to the wild type enzyme
G304S
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no inhibition by allosteric ligands, mechanism
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C256R
site-directed mutagenesis, mutation Gyk766AtoG, inactive mutant
E398D
naturally occurring mutation in patients with glyceroluria, causes a strong decrease in enzyme activity
G280A
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naturally occurring mutation in a patient with glyceroluria, causes a strong decrease in enzyme activity, mutation affects a highly conserved amino acid in the ATP-binding domain
L61P
naturally occurring mutation in patients with glyceroluria, causes an 5-10-fold increased Km for glycerol
M428T
site-directed mutagenesis, mutation Gyk1283TtoC, inactive mutant
A137S
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affinity for substrates increased 3-4 fold
D20A
about 95% activity compared to the wild type enzyme
E478A
about 25% activity compared to the wild type enzyme
M1A
about 90% activity compared to the wild type enzyme
R22A
about 60% activity compared to the wild type enzyme
R24A
about 30% activity compared to the wild type enzyme
T12V
less than 5% activity compared to the wild type enzyme
T273V
about 80% activity compared to the wild type enzyme
Y3F
about 80% activity compared to the wild type enzyme
S329D
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increase in thermostability, increase in Km by 100%
S329D
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mechanism of stabilization
H232A
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lacks the site of activation by phosphorylation, activity similar to unphosphorylated native enzyme
H232A
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residue located in the activation loop
A65T
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crystal structure
A65T
oligomeric interactions are disturbed by the amino acid substitution
G230D
structural analysis reveal that the decreased allosteric regulation in the G230D mutant is a result of the altered fructose 1,6-bisphosphate binding loop conformations in the mutant that interfere with the wild-type fructose 1,6-bisphosphate binding site. The altered fructose 1,6-bisphosphate binding loop conformation in the G230D mutant of glycerol kinase are supported through a series of intramolecular loop interactions. The appearence of Asp230 in the fructose 1,6-bisphosphate binding loops also repositions the wildtype fructose 1,6-bisphosphate binding residues away from the fructose 1,6-bisphosphate binging site.
G230D
hyperactive mutant enzyme
K271E
site-directed mutagenesis, the mutation disrupts the hexamer formation interface
K271E
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site-directed mutagenesis, the mutation disrupts the hexamer formation interface
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K271E
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site-directed mutagenesis, the mutation disrupts the hexamer formation interface
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additional information
knockout glcA in the DELTAgfdA and the parental wild-type strain backgrounds. The glcA null mutant shows defects of growth and conidiation in glycerol media but not in glucose media, suggesting glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media. In glucose medium, DELTAgfdADELTAglcA colonies are very small, and colonies are nearly undetectable colonies in the glycerol medium. Transformation of the full-length ORF sequence of glcA under the control of the constitutive promoter gpdA into the DELTAgfdA and reference strains, resulting in two glcA-overexpression strains, DELTAgfdAOE::glcA and wild-type OE::glcA. Overexpressed glcA is able to rescue growth defects associated with loss of gfdA. In comparison, wild-type OE::glcA still shows wild-type like colony phenotypes. Overexpression of glcA may result in the production of accumulated glycerol 3-phosphate (G3P), which allows colonies to bypass the requirement of gfdA to produce glycerol use in colony growth, indicating that the growth defects of gfdA null mutant might be due to absence of G3P rather than glycerol. In contrast, when glycerol is used as the sole carbon source, DELTAgfdAOE::glcA shows defective phenotypes similar to wild-type OE::glcA, indicating the overexpression of glcA may cause the production of accumulated G3P, which results in growth defects in glycerol media either in the presence or absence of gfdA
additional information
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knockout glcA in the DELTAgfdA and the parental wild-type strain backgrounds. The glcA null mutant shows defects of growth and conidiation in glycerol media but not in glucose media, suggesting glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media. In glucose medium, DELTAgfdADELTAglcA colonies are very small, and colonies are nearly undetectable colonies in the glycerol medium. Transformation of the full-length ORF sequence of glcA under the control of the constitutive promoter gpdA into the DELTAgfdA and reference strains, resulting in two glcA-overexpression strains, DELTAgfdAOE::glcA and wild-type OE::glcA. Overexpressed glcA is able to rescue growth defects associated with loss of gfdA. In comparison, wild-type OE::glcA still shows wild-type like colony phenotypes. Overexpression of glcA may result in the production of accumulated glycerol 3-phosphate (G3P), which allows colonies to bypass the requirement of gfdA to produce glycerol use in colony growth, indicating that the growth defects of gfdA null mutant might be due to absence of G3P rather than glycerol. In contrast, when glycerol is used as the sole carbon source, DELTAgfdAOE::glcA shows defective phenotypes similar to wild-type OE::glcA, indicating the overexpression of glcA may cause the production of accumulated G3P, which results in growth defects in glycerol media either in the presence or absence of gfdA
additional information
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knockout glcA in the DELTAgfdA and the parental wild-type strain backgrounds. The glcA null mutant shows defects of growth and conidiation in glycerol media but not in glucose media, suggesting glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media. In glucose medium, DELTAgfdADELTAglcA colonies are very small, and colonies are nearly undetectable colonies in the glycerol medium. Transformation of the full-length ORF sequence of glcA under the control of the constitutive promoter gpdA into the DELTAgfdA and reference strains, resulting in two glcA-overexpression strains, DELTAgfdAOE::glcA and wild-type OE::glcA. Overexpressed glcA is able to rescue growth defects associated with loss of gfdA. In comparison, wild-type OE::glcA still shows wild-type like colony phenotypes. Overexpression of glcA may result in the production of accumulated glycerol 3-phosphate (G3P), which allows colonies to bypass the requirement of gfdA to produce glycerol use in colony growth, indicating that the growth defects of gfdA null mutant might be due to absence of G3P rather than glycerol. In contrast, when glycerol is used as the sole carbon source, DELTAgfdAOE::glcA shows defective phenotypes similar to wild-type OE::glcA, indicating the overexpression of glcA may cause the production of accumulated G3P, which results in growth defects in glycerol media either in the presence or absence of gfdA
-
additional information
-
knockout glcA in the DELTAgfdA and the parental wild-type strain backgrounds. The glcA null mutant shows defects of growth and conidiation in glycerol media but not in glucose media, suggesting glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media. In glucose medium, DELTAgfdADELTAglcA colonies are very small, and colonies are nearly undetectable colonies in the glycerol medium. Transformation of the full-length ORF sequence of glcA under the control of the constitutive promoter gpdA into the DELTAgfdA and reference strains, resulting in two glcA-overexpression strains, DELTAgfdAOE::glcA and wild-type OE::glcA. Overexpressed glcA is able to rescue growth defects associated with loss of gfdA. In comparison, wild-type OE::glcA still shows wild-type like colony phenotypes. Overexpression of glcA may result in the production of accumulated glycerol 3-phosphate (G3P), which allows colonies to bypass the requirement of gfdA to produce glycerol use in colony growth, indicating that the growth defects of gfdA null mutant might be due to absence of G3P rather than glycerol. In contrast, when glycerol is used as the sole carbon source, DELTAgfdAOE::glcA shows defective phenotypes similar to wild-type OE::glcA, indicating the overexpression of glcA may cause the production of accumulated G3P, which results in growth defects in glycerol media either in the presence or absence of gfdA
-
additional information
-
knockout glcA in the DELTAgfdA and the parental wild-type strain backgrounds. The glcA null mutant shows defects of growth and conidiation in glycerol media but not in glucose media, suggesting glcA is required when glycerol is the sole carbon source, and gfdA is required when glucose is the sole carbon source. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media. In glucose medium, DELTAgfdADELTAglcA colonies are very small, and colonies are nearly undetectable colonies in the glycerol medium. Transformation of the full-length ORF sequence of glcA under the control of the constitutive promoter gpdA into the DELTAgfdA and reference strains, resulting in two glcA-overexpression strains, DELTAgfdAOE::glcA and wild-type OE::glcA. Overexpressed glcA is able to rescue growth defects associated with loss of gfdA. In comparison, wild-type OE::glcA still shows wild-type like colony phenotypes. Overexpression of glcA may result in the production of accumulated glycerol 3-phosphate (G3P), which allows colonies to bypass the requirement of gfdA to produce glycerol use in colony growth, indicating that the growth defects of gfdA null mutant might be due to absence of G3P rather than glycerol. In contrast, when glycerol is used as the sole carbon source, DELTAgfdAOE::glcA shows defective phenotypes similar to wild-type OE::glcA, indicating the overexpression of glcA may cause the production of accumulated G3P, which results in growth defects in glycerol media either in the presence or absence of gfdA
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additional information
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co-immobilization of nanoparticles of lipase, glycerol kinase and glycerol 3-phosphate oxidase onto pencil graphite electrode, function as improved amperometric triglyceride biosensor. An improved amperometric triglyceride (TG) biosensor is fabricated using lipaseNPs/GKNPs/GPONPs/PG electrode as the working electrode, Ag/AgCl as the standard electrode and Pt wire as auxiliary electrode. The biosensor shows optimum response within 2.5 s at pH 7.0 and temperature of 35°C. The biosensor measures current due to electrons generated at 0.1 V against Ag/AgCl, from H2O2, which is produced from triolein by co-immobilized enzyme nanoparticles (ENPs). The biosensor is evaluated and employed for determination of triglyceride in the serum of apparently healthy subject and persons suffering from hypertriglyceridemia. The biosensor loses 20% of its initial activity after continued uses over a period of 240 days, while being stored at 4°C. Construction of the biosensor, evaluation, and optimization, overview
additional information
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rational design of nanoparticle platforms for cutting-the-fat, covalent immobilization of lipase, glycerol kinase, and glycerol-3-phosphate oxidase on metal nanoparticles. Co-immobilization of enzymes onto nanoparticles aggregates is expected to produce faster kinetics than their individual immobilizations on separate matrices. The combined activities of co-immobilized enzymes are tested amperometrically, and these composite nanobiocatalysts show optimum activity within 4-5 s, at pH 6.5-7.5 and 35°C, when polarized at a potential between 0.1 and 0.4 V. Co-immobilized enzymes show excellent linearity within 50-700 mg/dl of the lipid with detection limit of 20 mg/dl for triolein. The half life of co-immobilized enzymes is 7 months, when stored dry at 4°C, which is very convenient for practical applications. Co-immobilized biocatalysts measured triglycerides (TGs) in the sera of apparently healthy persons and persons suffering from hypertriglyceridemia, which is recognized as a leading cause for heart disease. The measurement of serum TG by co-immobilized enzymes is unaffected by the presence of a number of serum substances, tested as potential interferences. Attachment of enzymes onto an insoluble support not only provides their reusability but also realizes the extra stabilization rendered by the multipoint covalent attachment or multisubunit binding of the enzymes on solid supports. Use of rationally designed nanoscaffolds for enzyme binding, method development, evaluation, and optimization, overview
additional information
a naturally occuring mutation in intron 3 causes the insertion of an additional exon
additional information
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a naturally occuring mutation in intron 3 causes the insertion of an additional exon
additional information
NR4A11-250, NR4A11-375, NR4A1251-375, NR4A1251-598, and NR4A1376-598 proteins are obtained from whole-cell lysates of HEK293 cells transfected with the corresponding vectors. Selected Gyk isoform b-targeting small interfering RNA (siRNA)1555 oligonucleotides. Gyk inhibits the effects of NR4A1 on hepatic gluconeogenesis in diabetic mice
additional information
silencing using short hairpin RNA (shRNA) vectors against the GK5 genes shGK5-1 and shGK5-2. shGK5-1 and -2 significantly inhibit GK5 expressions. Morphological examination shows that GK5 knockdown reduces the number of PC9R cells transfected with shGK5 compared to those transfected with negative control shRNA for 24 h and then treated with 0.001 mM gefitinib for 72 h. The CCK8 assays reveals that transfection of PC9R cells with either shGK5-1 or -2 enhances gefitinib-induced apoptosis. GK5 knockdown induces PC9R cell apoptosis and cell cycle arrest in the presence of gefitinib
additional information
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silencing using short hairpin RNA (shRNA) vectors against the GK5 genes shGK5-1 and shGK5-2. shGK5-1 and -2 significantly inhibit GK5 expressions. Morphological examination shows that GK5 knockdown reduces the number of PC9R cells transfected with shGK5 compared to those transfected with negative control shRNA for 24 h and then treated with 0.001 mM gefitinib for 72 h. The CCK8 assays reveals that transfection of PC9R cells with either shGK5-1 or -2 enhances gefitinib-induced apoptosis. GK5 knockdown induces PC9R cell apoptosis and cell cycle arrest in the presence of gefitinib
additional information
recombinant expression of GST-tagged wild-type and mutant KPN00353s in Klebsiella pneumoniae strain MGH 78578. Protein pull-down assay, GST-tagged GlpK binds to His-tagged H65D or His-tagged H65E mutant proteins more strongly than to His-tagged H65R or to His-tagged wild-type KPN00353 and binds weakly to His-tagged H65Q. The binding affinity between GlpK and the His-tagged H110Q mutant protein is similar to that between GlpK and His-tagged wild-type KPN00353. Quantification of intracellular G3P in recombinant Klebsiella pneumoniae overexpressing wild-type or variant KPN00353 proteins. Interaction analysis with wild-type and mutant variants of regulator KPN00353, KPN00353 H65 mutants (H65D, H65E, H65Q, and H65R) overexpression leads to altered intracellular glycerol-3-phosphate concentration in the cells compared to wild-type KPN00353
additional information
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recombinant expression of GST-tagged wild-type and mutant KPN00353s in Klebsiella pneumoniae strain MGH 78578. Protein pull-down assay, GST-tagged GlpK binds to His-tagged H65D or His-tagged H65E mutant proteins more strongly than to His-tagged H65R or to His-tagged wild-type KPN00353 and binds weakly to His-tagged H65Q. The binding affinity between GlpK and the His-tagged H110Q mutant protein is similar to that between GlpK and His-tagged wild-type KPN00353. Quantification of intracellular G3P in recombinant Klebsiella pneumoniae overexpressing wild-type or variant KPN00353 proteins. Interaction analysis with wild-type and mutant variants of regulator KPN00353, KPN00353 H65 mutants (H65D, H65E, H65Q, and H65R) overexpression leads to altered intracellular glycerol-3-phosphate concentration in the cells compared to wild-type KPN00353
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additional information
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recombinant expression of GST-tagged wild-type and mutant KPN00353s in Klebsiella pneumoniae strain MGH 78578. Protein pull-down assay, GST-tagged GlpK binds to His-tagged H65D or His-tagged H65E mutant proteins more strongly than to His-tagged H65R or to His-tagged wild-type KPN00353 and binds weakly to His-tagged H65Q. The binding affinity between GlpK and the His-tagged H110Q mutant protein is similar to that between GlpK and His-tagged wild-type KPN00353. Quantification of intracellular G3P in recombinant Klebsiella pneumoniae overexpressing wild-type or variant KPN00353 proteins. Interaction analysis with wild-type and mutant variants of regulator KPN00353, KPN00353 H65 mutants (H65D, H65E, H65Q, and H65R) overexpression leads to altered intracellular glycerol-3-phosphate concentration in the cells compared to wild-type KPN00353
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additional information
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Aqp7-/- knock out mice. Gene replacement targeting strategy is used to inactivate the Aqp7 gene in R1 mouse ES cells. Targeted ES cell clones are injected into blastocysts of C57BL/6J mice. Glycerol kinase expression (mRNA level) and activity is increased in pancreatic islets of Aqp7-/- mice compared to Aqp+/+ mice.
additional information
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Aqp7-knockout mice
additional information
generation of Gk2-7/-7 KO mice using the CRISPR/Cas9 system, analysis of sperm mitochondria in testis using a freeze-fracture method with scanning electron microscopy. To generate the Gk2 KO mice, the pX330 plasmid is prepared expressing a chimeric sgRNA together with human codon-optimized Cas9 (hCas9) by ligating oligonucleotides into the BbsI site. The sgRNAs recognize sequences close to the start codon. Gk2-disrupted spermatids show abnormal localization of crescent-like mitochondria, in spite of the initial proper alignment of spherical mitochondria around the flagellum, which causes abnormal mitochondrial sheath formation leading to exposure of the outer dense fibers. Phenotype of Gk2-7/-7 mice, overview
additional information
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generation of Gk2-7/-7 KO mice using the CRISPR/Cas9 system, analysis of sperm mitochondria in testis using a freeze-fracture method with scanning electron microscopy. To generate the Gk2 KO mice, the pX330 plasmid is prepared expressing a chimeric sgRNA together with human codon-optimized Cas9 (hCas9) by ligating oligonucleotides into the BbsI site. The sgRNAs recognize sequences close to the start codon. Gk2-disrupted spermatids show abnormal localization of crescent-like mitochondria, in spite of the initial proper alignment of spherical mitochondria around the flagellum, which causes abnormal mitochondrial sheath formation leading to exposure of the outer dense fibers. Phenotype of Gk2-7/-7 mice, overview
additional information
frameshift mutations in a hypervariable homopolymeric region of the glpK gene are a specific marker of multidrug resistance in clinical Mycobacterium tuberculosis isolates, and these loss-of-function alleles are also enriched in extensively drug-resistant clones. Reversible high-frequency variation in carbon metabolic pathways can produce phenotypically drug-tolerant clones and have a role in the development of resistance. Construction of a DELTAglpK mutant, that is significantly less sensitive to isoniazid (INH) and rifampin (RIF) than the wild-type or the complemented mutant
additional information
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frameshift mutations in a hypervariable homopolymeric region of the glpK gene are a specific marker of multidrug resistance in clinical Mycobacterium tuberculosis isolates, and these loss-of-function alleles are also enriched in extensively drug-resistant clones. Reversible high-frequency variation in carbon metabolic pathways can produce phenotypically drug-tolerant clones and have a role in the development of resistance. Construction of a DELTAglpK mutant, that is significantly less sensitive to isoniazid (INH) and rifampin (RIF) than the wild-type or the complemented mutant
additional information
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frameshift mutations in a hypervariable homopolymeric region of the glpK gene are a specific marker of multidrug resistance in clinical Mycobacterium tuberculosis isolates, and these loss-of-function alleles are also enriched in extensively drug-resistant clones. Reversible high-frequency variation in carbon metabolic pathways can produce phenotypically drug-tolerant clones and have a role in the development of resistance. Construction of a DELTAglpK mutant, that is significantly less sensitive to isoniazid (INH) and rifampin (RIF) than the wild-type or the complemented mutant
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additional information
overexpression of glycerol kinase under oxidative stress with glycerol supplementation leads to enhancement of lipid production in Synechocystis sp. PCC 6803
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Geobacillus stearothermophilus
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Debaryomyces hansenii
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Enterococcus casseliflavus
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Crystallization and preliminary x-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis
Acta Crystallogr. Sect. F
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2007
Thermococcus kodakarensis
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5722-5731
2007
Escherichia coli (P0A6F3), Escherichia coli
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Rattus norvegicus
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Conserved family of glycerol kinase loci in Drosophila melanogaster
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Drosophila melanogaster
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Hibuse, T.; Maeda, N.; Funahashi, T.; Yamamoto, K.; Nagasawa, A.; Mizunoya, W.; Kishida, K.; Inoue, K.; Kuriyama, H.; Nakamura, T.; Fushiki, T.; Kihara, S.; Shimomura, I.
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Proc. Natl. Acad. Sci. USA
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10993-10998
2005
Mus musculus
brenda
Katsumi, R.; Koga, Y.; You, D.J.; Matsumura, H.; Takano, K.; Kanaya, S.
Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis
Acta Crystallogr. Sect. F
63
126-129
2007
Thermococcus kodakarensis (O93623), Thermococcus kodakarensis
brenda
Yu, P.; Lasagna, M.; Pawlyk, A.C.; Reinhart, G.D.; Pettigrew, D.W.
IIAGlc inhibition of glycerol kinase: a communications network tunes protein motions at the allosteric site
Biochemistry
46
12355-12365
2007
Escherichia coli (P0A6F3), Escherichia coli
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Aragon Casale, C.; Ferreira-Dias, S.; Gattas Aparecida de Lucca, E.; Maristela de Freitas Sanches, P.
Characterization of glycerol kinase from bakers yeast: Response surface modeling of the enzymatic reaction
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2008
Saccharomyces cerevisiae
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Pettigrew, D.W.
Amino acid substitutions in the sugar kinase/hsp70/actin superfamily conserved ATPase core of E. coli glycerol kinase modulate allosteric ligand affinity but do not alter allosteric coupling
Arch. Biochem. Biophys.
481
151-156
2009
Escherichia coli
brenda
Pettigrew, D.W.
Oligomeric interactions provide alternatives to direct steric modes of control of sugar kinase/actin/hsp70 superfamily functions by heterotropic allosteric effectors: inhibition of E. coli glycerol kinase
Arch. Biochem. Biophys.
492
29-39
2009
Escherichia coli (P0A6F3), Escherichia coli
brenda
Yeh, J.I.; Kettering, R.; Saxl, R.; Bourand, A.; Darbon, E.; Joly, N.; Briozzo, P.; Deutscher, J.
Structural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation
Biochemistry
48
346-356
2009
Enterococcus casseliflavus
brenda
Kihara, F.; Itoh, K.; Iwasaka, M.; Niimi, T.; Yamashita, O.; Yaginuma, T.
Glycerol kinase activity and glycerol kinase-3 gene are up-regulated by acclimation to 5 degrees C in diapause eggs of the silkworm, Bombyx mori
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39
763-769
2009
Bombyx mori (B0I1G6), Bombyx mori (B0M0V1), Bombyx mori
brenda
Sherwood, K.E.; Cano, D.J.; Maupin-Furlow, J.A.
Glycerol-mediated repression of glucose metabolism and glycerol kinase as the sole route of glycerol catabolism in the haloarchaeon Haloferax volcanii
J. Bacteriol.
191
4307-4315
2009
Haloferax volcanii
brenda
Okawara, S.; Hamano, S.; Tetsuka, M.
Bovine oocytes and early embryos express mRNA encoding glycerol kinase but addition of glycerol to the culture media interferes with oocyte maturation
J. Reprod. Dev.
55
177-182
2009
Bos taurus (Q0IID9), Bos taurus
brenda
Sriram, G.; Rahib, L.; He, J.; Campos, A.; Parr, L.; Liao, J.; Dipple, K.
Global metabolic effects of glycerol kinase overexpression in rat hepatoma cells
Mol. Genet. Metab.
93
145-159
2008
Rattus norvegicus
brenda
Rahib, L.; Sriram, G.; Harada, M.K.; Liao, J.C.; Dipple, K.M.
Transcriptomic and network component analysis of glycerol kinase in skeletal muscle using a mouse model of glycerol kinase deficiency
Mol. Genet. Metab.
96
106-112
2009
Mus musculus
brenda
MacLennan, N.K.; Dong, J.; Aten, J.E.; Horvath, S.; Rahib, L.; Ornelas, L.; Dipple, K.M.; McCabe, E.R.
Weighted gene co-expression network analysis identifies biomarkers in glycerol kinase deficient mice
Mol. Genet. Metab.
98
203-214
2009
Mus musculus
brenda
Schnick, C.; Polley, S.D.; Fivelman, Q.L.; Ranford-Cartwright, L.C.; Wilkinson, S.R.; Brannigan, J.A.; Wilkinson, A.J.; Baker, D.A.
Structure and non-essential function of glycerol kinase in Plasmodium falciparum blood stages
Mol. Microbiol.
71
533-545
2009
Plasmodium falciparum (Q8IDI4), Plasmodium falciparum
brenda
Walmsley, T.A.; Potter, H.C.; George, P.M.; Florkowski, C.M.
Pseudo-hypertriglyceridaemia: a measurement artefact due to glycerol kinase deficiency
Postgrad. Med. J.
84
552-554
2008
Homo sapiens
brenda
Balogun, E.O.; Inaoka, D.K.; Kido, Y.; Shiba, T.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Michels, P.A.; Harada, S.; Kita, K.
Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Trypanosoma brucei gambiense glycerol kinase
Acta Crystallogr. Sect. F
66
304-308
2010
Trypanosoma brucei gambiense (D3KVM3), Trypanosoma brucei gambiense, Trypanosoma brucei gambiense IL2343 (D3KVM3)
brenda
Ditlecadet, D.; Short, C.E.; Driedzic, W.R.
Glycerol loss to water exceeds glycerol catabolism via glycerol kinase in freeze-resistant rainbow smelt (Osmerus mordax)
Am. J. Physiol. Regul. Integr. Comp. Physiol.
300
R674-R684
2011
Osmerus mordax
brenda
Ahmad, I.; Shim, W.Y.; Kim, J.H.
Enhancement of xylitol production in glycerol kinase disrupted Candida tropicalis by co-expression of three genes involved in glycerol metabolic pathway
Bioprocess Biosyst. Eng.
36
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2013
Candida tropicalis, Candida tropicalis BSXDH-3
brenda
Aizemberg, R.; Terrazas, W.; Ferreira-Dias, S.; Valentini, S.; Gattas, E.
Optimal conditions for biomass and recombinant glycerol kinase production using the yeast Pichia pastoris
Food Technol. Biotechnol.
49
329-335
2011
Saccharomyces cerevisiae
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brenda
Applebee, M.K.; Joyce, A.R.; Conrad, T.M.; Pettigrew, D.W.; Palsson, B.O.
Functional and metabolic effects of adaptive glycerol kinase (GLPK) mutants in Escherichia coli
J. Biol. Chem.
286
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2011
Escherichia coli
brenda
Restiawaty, E.; Honda, K.; Okano, K.; Hirota, R.; Omasa, T.; Kuroda, A.; Ohtake, H.
Construction of membrane-anchoring fusion protein of Thermococcus kodakaraensis glycerol kinase and its application to repetitive batchwise reactions
J. Biosci. Bioeng.
113
521-525
2012
Thermococcus kodakarensis
brenda
Ohashi-Suzuki, M.; Yabu, Y.; Ohshima, S.; Nakamura, K.; Kido, Y.; Sakamoto, K.; Kita, K.; Ohta, N.; Suzuki, T.
Differential kinetic activities of glycerol kinase among African trypanosome species: phylogenetic and therapeutic implications
J. Vet. Med. Sci.
73
615-621
2011
Trypanosoma vivax (B0I530), Trypanosoma vivax, Trypanosoma congolense (Q75T26), Trypanosoma congolense, Trypanosoma brucei brucei (Q9NJP9), Trypanosoma congolense IL1180 (Q75T26), Trypanosoma brucei brucei ILTat1.4 (Q9NJP9), Trypanosoma vivax IL1392 (B0I530)
brenda
Sriram, G.; Parr, L.S.; Rahib, L.; Liao, J.C.; Dipple, K.M.
Moonlighting function of glycerol kinase causes systems-level changes in rat hepatoma cells
Metab. Eng.
12
332-340
2010
Homo sapiens
brenda
Balogun, E.O.; Inaoka, D.K.; Shiba, T.; Kido, Y.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Michels, P.A.; Harada, S.; Kita, K.
Biochemical characterization of highly active Trypanosoma brucei gambiense glycerol kinase, a promising drug target
J. Biochem.
154
77-84
2013
Trypanosoma brucei gambiense
brenda
Rodriguez-Contreras, D.; Hamilton, N.
Gluconeogenesis in Leishmania mexicana: contribution of glycerol kinase, phosphoenolpyruvate carboxykinase, and pyruvate phosphate dikinase
J. Biol. Chem.
289
32989-33000
2014
Leishmania mexicana
brenda
Fukuda, Y.; Abe, A.; Tamura, T.; Kishimoto, T.; Sogabe, A.; Akanuma, S.; Yokobori, S.; Yamagishi, A.; Imada, K.; Inagaki, K.
Epistasis effects of multiple ancestral-consensus amino acid substitutions on the thermal stability of glycerol kinase from Cellulomonas sp. NT3060
J. Biosci. Bioeng.
121
497-502
2016
Cellulomonas sp. (D0VZG4), Cellulomonas sp. NT3060 (D0VZG4)
brenda
Jeong, C.Y.; Han, Y.D.; Yoon, J.H.; Yoon, H.C.
Bioelectrocatalytic sensor for triglycerides in human skin sebum based on enzymatic cascade reaction of lipase, glycerol kinase and glycerophosphate oxidase
J. Biotechnol.
175
7-14
2014
Homo sapiens
brenda
Park, Y.; Kim, Y.
A specific glycerol kinase induces rapid cold hardening of the diamondback moth, Plutella xylostella
J. Insect Physiol.
67
56-63
2014
Plutella xylostella
brenda
Balogun, E.O.; Inaoka, D.K.; Shiba, T.; Kido, Y.; Tsuge, C.; Nara, T.; Aoki, T.; Honma, T.; Tanaka, A.; Inoue, M.; Matsuoka, S.; Michels, P.A.; Kita, K.; Harada, S.
Molecular basis for the reverse reaction of African human trypanosomes glycerol kinase
Mol. Microbiol.
94
1315-1329
2014
Trypanosoma brucei gambiense (D3KVM3)
brenda
Terrazas, W.; Aizemberg, R.; Gattas, E.
Using Pichia pastoris to produce recombinant glycerol kinase
Rev. Cienc. Farm. Basica Apl.
35
279-284
2014
Saccharomyces cerevisiae
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brenda
Yokobori, S.I.; Nakajima, Y.; Akanuma, S.; Yamagishi, A.
Birth of archaeal cells molecular phylogenetic analyses of G1P dehydrogenase, G3P dehydrogenases, and glycerol kinase suggest derived features of archaeal membranes having G1P polar lipids
Archaea
2016
1802675
2016
Escherichia coli (P0A6F3)
brenda
Balogun, E.O.; Inaoka, D.K.; Shiba, T.; Tokuoka, S.M.; Tokumasu, F.; Sakamoto, K.; Kido, Y.; Michels, P.A.M.; Watanabe, Y.I.; Harada, S.; Kita, K.
Glycerol kinase of African trypanosomes possesses an intrinsic phosphatase activity
Biochim. Biophys. Acta
1861
2830-2842
2017
Trypanosoma brucei gambiense (D3KVM3), Trypanosoma brucei gambiense, Trypanosoma brucei rhodesiense (D3KVM4)
brenda
Sivaramakrishnan, R.; Incharoensakdi, A.
Enhancement of lipid production in Synechocystis sp. PCC 6803 overexpressing glycerol kinase under oxidative stress with glycerol supplementation
Biores. Technol.
267
532-540
2018
Synechocystis sp. PCC 6803 (P74260)
brenda
Narwal, V.; Pundir, C.S.
An improved amperometric triglyceride biosensor based on co-immobilization of nanoparticles of lipase, glycerol kinase and glycerol 3-phosphate oxidase onto pencil graphite electrode
Enzyme Microb. Technol.
100
11-16
2017
Cellulomonas sp.
brenda
Miao, L.; Yang, Y.; Liu, Y.; Lai, L.; Wang, L.; Zhan, Y.; Yin, R.; Yu, M.; Li, C.; Yang, X.; Ge, C.
Glycerol kinase interacts with nuclear receptor NR4A1 and regulates glucose metabolism in the liver
FASEB J.
33
6736-6747
2019
Homo sapiens (P32189)
brenda
Jeng, W.Y.; Panjaitan, N.S.D.; Horng, Y.T.; Chung, W.T.; Chien, C.C.; Soo, P.C.
The negative effects of KPN00353 on glycerol kinase and microaerobic 1,3-propanediol production in Klebsiella pneumoniae
Front. Microbiol.
8
2441
2017
Klebsiella pneumoniae subsp. pneumoniae (A6TFR2), Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 (A6TFR2), Klebsiella pneumoniae subsp. pneumoniae MGH 78578 (A6TFR2)
brenda
Zhang, C.; Meng, X.; Gu, H.; Ma, Z.; Lu, L.
Predicted glycerol 3-phosphate dehydrogenase homologs and the glycerol kinase GlcA coordinately adapt to various carbon sources and osmotic stress in Aspergillus fumigatus
G3 (Bethesda)
8
2291-2299
2018
Aspergillus fumigatus (B0Y6Y4), Aspergillus fumigatus, Aspergillus fumigatus CBS 144.89 (B0Y6Y4), Aspergillus fumigatus CEA10 (B0Y6Y4), Aspergillus fumigatus FGSC A1163 (B0Y6Y4)
brenda
Hokao, R.; Matsumura, H.; Katsumi, R.; Angkawidjaja, C.; Takano, K.; Kanaya, S.; Koga, Y.
Affinity shift of ATP upon glycerol binding to a glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1
J. Biosci. Bioeng.
129
657-663
2020
Thermococcus kodakarensis (O93623), Thermococcus kodakarensis, Thermococcus kodakarensis JCM 12380 (O93623), Thermococcus kodakarensis ATCC BAA-918 (O93623)
brenda
Zhou, J.; Qu, G.; Zhang, G.; Wu, Z.; Liu, J.; Yang, D.; Li, J.; Chang, M.; Zeng, H.; Hu, J.; Fang, T.; Song, Y.; Bai, C.
Glycerol kinase 5 confers gefitinib resistance through SREBP1/SCD1 signaling pathway
J. Exp. Clin. Cancer Res.
38
96
2019
Homo sapiens (Q6ZS86), Homo sapiens
brenda
Shimada, K.; Kato, H.; Miyata, H.; Ikawa, M.
Glycerol kinase 2 is essential for proper arrangement of crescent-like mitochondria to form the mitochondrial sheath during mouse spermatogenesis
J. Reprod. Dev.
65
155-162
2019
Mus musculus (Q9WU65), Mus musculus
brenda
Bellerose, M.M.; Baek, S.H.; Huang, C.C.; Moss, C.E.; Koh, E.I.; Proulx, M.K.; Smith, C.M.; Baker, R.E.; Lee, J.S.; Eum, S.; Shin, S.J.; Cho, S.N.; Murray, M.; Sassetti, C.M.
Common variants in the glycerol kinase gene reduce tuberculosis drug efficacy
mBio
10
e00663-19
2019
Mycobacterium tuberculosis (P9WPK1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPK1)
brenda
Aggarwal, V.; Pundir, C.S.
Rational design of nanoparticle platforms for cutting-the-fat covalent immobilization of lipase, glycerol kinase, and glycerol-3-phosphate oxidase on metal nanoparticles
Methods Enzymol.
571
197-223
2016
Cellulomonas sp.
brenda
Molla, G.; Himmelspach, A.; Wohlgemuth, R.; Haupt, E.; Liese, A.
Mechanistic and kinetics elucidation of Mg2+/ATP molar ratio effect on glycerol kinase
Mol. Catal.
445
36-42
2018
Cellulomonas sp.
-
brenda