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Information on EC 3.1.3.9 - glucose-6-phosphatase and Organism(s) Homo sapiens and UniProt Accession Q9NQR9

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.9 glucose-6-phosphatase
IUBMB Comments
Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate---hexose phosphotransferase), EC 2.7.1.79 (diphosphate---glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: Q9NQR9
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
D-glucose-6-phosphate phosphorylase, G-6-Pase, G6Pase, G6Pase-alpha, G6PC, G6PC-2, G6PC-3, G6Pc1, G6PC2, Glc-6-P phosphohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G-6-Pase
-
-
-
-
G6Pase
G6Pase-alpha
288509
-
G6PC2
glucose 6-phosphate phosphatase
-
-
-
-
glucose 6-phosphate phosphohydrolase
-
-
-
-
glucose-6-phosphatase
247
-
glucose-6-phosphatase catalytic subunit 2
288506
-
glucose-6-phosphatase catalytic subunit-related protein
247
-
glucose-6-phosphatase catalytic unit 2
247
-
glucose-6-phosphatase-alpha
islet-specific glucose-6-phosphatase catalytic subunit-related protein
247
-
islet-specific glucose-6-phosphatase-related protein
288506
-
phosphatase, glucose 6-
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glucose 6-phosphate + H2O = D-glucose + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate phosphohydrolase
Wide distribution in animal tissues. Also catalyses potent transphosphorylations from carbamoyl phosphate, hexose phosphates, diphosphate, phosphoenolpyruvate and nucleoside di- and triphosphates, to D-glucose, D-mannose, 3-methyl-D-glucose or 2-deoxy-D-glucose [cf. EC 2.7.1.62 (phosphoramidate---hexose phosphotransferase), EC 2.7.1.79 (diphosphate---glycerol phosphotransferase) and EC 3.9.1.1 (phosphoamidase)].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-39-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
show the reaction diagram
a better substrate in disrupted vesicles at pH 5.5 and pH 6.5
-
?
carbamoyl-phosphate + glucose
glucose 6-phosphate + NH3 + CO2
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-mannose 6-phosphate + H2O
D-mannose + phosphate
show the reaction diagram
-
-
-
?
diphosphate + glucose
glucose 6-phosphate + phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
best substrate in disrupted and not disrupted vesicles at pH 5.5 and pH 6.5
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4-dicaffeoylquinic acid
-
-
3-Mercaptopicolinic acid
-
inhibitor of D-glucose 6-phosphate translocase
4,4'-di-isothiocyanostilbene-2,2'-disulphonate
-
inhibitor of D-glucose 6-phosphate translocase
4,5-dicaffeoylquinic acid
-
-
4-caffeoylquinic acid
-
-
5-caffeoylquinic acid
-
-
chlorogenic acid
-
inhibitor of D-glucose 6-phosphate translocase
D-glucose
-
non-competitive inhibitor, irrespective of the presence of detergents
Insulin
-
insulin causes a decrease in the activity of enzyme in the liver in vivo
-
kodaistatin A
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A and C
mumbaistatin
-
-
phosphate
-
non-competitive inhibition in intact microsomes, but competitive in the presence of detergents
Svetol
-
commercial unroasted and decaffeinated green Coffea canephora extract, competive inhibition
-
tosyl-lysyl-chloromethane
-
inhibitor of D-glucose 6-phosphate translocase
tosylphenylalanylchloromethane
-
inhibitor of D-glucose 6-phosphate translocase
tungstate
-
-
vanadate
-
-
additional information
-
The enzyme is inhibited by several amphiphilic compounds, such as fatty acids and acyl-CoAs, but the physioligal significance is questionable, since the liver contains a fatty-acyl CoA binding protein, which may well prevent this effect. Some thiol reagents inhibit enzyme activity much more in intact than in disrupted microsomes.
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose
-
elevated concentration, D-glucose may play a direct role as a stimulator of enzyme expression
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 4.3
D-glucose 6-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
4,4'-di-isothiocyanostilbene-2,2'-disulphonate
-
-
0.5
chlorogenic acid
-
-
50 - 200
D-glucose
-
-
0.001 - 0.025
tungstate
0.0022 - 0.0056
vanadate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
3,4-dicaffeoylquinic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0078
purified FLAG-tagged recombinant mutant T16R
0.008
purified detagged recombinant mutant T16R
0.0083
purified detagged or FLAG-tagged recombinant mutant Y209C
0.051
-
enzyme from liver
0.068
purified FLAG-tagged recombinant wild-type enzyme
0.095
-
liver microsomes
0.102
-
activity using pSVL expression system
0.136
purified detagged recombinant wild-type enzyme
0.335
-
enzyme from microsomes, at 25°C
0.5473
-
enzyme from octylglucoside-solubilized extract, at 25°C
1.065
-
enzyme from proteoliposomes dialyzed against MOPS buffer, at 25°C
1.268
-
activity using adenoviral expression system
6.58
-
enzyme from placenta
67.7
recombinant FLAG-tagged wild-type enzyme
136
recombinant non-tagged wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
-
-
6
in disruptes vesicles
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low enzyme activities
Manually annotated by BRENDA team
expression of G6PC3 isoform
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
G6PC2_HUMAN
355
7
40580
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38730
calculation from sequence of cDNA
40000
-
Western blot analysis
41000
-
Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
side-chain modification
-
enzyme is active as a phosphoprotein, dephosphorylation leads to inactivation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D38V
-
the mutation leads to reduced levels of G6PC protein
E110Q
-
the mutation retains 16% of wild type activity
F322L
-
mutant has similar stability to wild type enzyme
F327del/V338F/I341N/L345R
-
the mutation leads to reduced levels of G6PC protein
G122D
-
mutant has similar stability to wild type enzyme
G188D/G188S/G188R
-
the mutation leads to reduced levels of G6PC protein
G222R
-
the mutation retains 2.6% of wild type activity
G350X
-
the mutation retains 41.5% of wild type activity
H119A
-
mutation inactivates the phosphatase
H119L
-
the mutation completely abolishes enzymatic activity
H176A
H179A
-
mutation completely abolishes the enzyme activity
H197T
-
no significant change of enzyme activity
H252A
-
no significant change of enzyme activity
H307A
-
no significant change of enzyme activity
H353A
-
no significant change of enzyme activity
H353X
-
the mutation retains 60% of wild type activity
H52A
-
no significant change of enzyme activity
H9A
-
no significant change of enzyme activity
K355X
-
the mutation retains 65% of wild type activity
L349X
-
the mutation retains 5.3% of wild type activity
N264K/L265P/G266V/G270V/G270R
-
the mutation leads to reduced levels of G6PC protein
P257L
-
the mutation retains 6.1% of wild type activity
Q347X
-
the mutation completely inactivates the G6PC enzyme
Q351X
-
the mutation retains 43% of wild type activity
Q54P
naturally occurring missense mutation, no phenotype; naturally occurring mutation of the enzyme from an argentinian glycogen storage disease type Ia patient
R170Q
R170X
-
the mutation completely inactivates the G6PC enzyme
R295C/S298P
-
the mutation leads to reduced levels of G6PC protein
R83H
-
the mutation completely abolishes enzymatic activity
T16A
site-directed mutagenesis, 74-78% reduced activity compared to the wild-type enzyme
T16R
naturally occurring N-terminal mutation of the enzyme from an argentinian glycogen storage disease type Ia patient, site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme; the isolated glucose-6-phosphatase mutation, in the sixth transmembrane helix, affects protein stability and causes glycogen storgae disease type Ia determined in Argentina, overview, the mutant constructed using site-sirected mutagenesis shows no enzymatic activity and reduced enzyme stability
V166A
-
the mutation leads to reduced levels of G6PC protein
W63R/G68R
-
the mutation leads to reduced levels of G6PC protein
Y209C
naturally occurring mutation in the sixth transmembrane helix of the enzyme from an argentinian glycogen storage disease type Ia patient, site-directed mutagenesis, about 90% reduced activity compared to the wild-type enzyme; the isolated glucose-6-phosphatase mutation, in the sixth transmembrane helix, affects protein stability and causes glycogen storgae disease type Ia determined in Argentina, overview, the mutant constructed using site-sirected mutagenesis shows no enzymatic activity and reduced enzyme stability
Y209C/L211P/G222R
-
the mutation leads to reduced levels of G6PC protein
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
The treatment with detergents, wheter anionic, cationic or neutral, modestly stimulates the hydrolysis of D-glucose 6-phosphate, but considerably increases the phosphatase activity on other substrates, such as mannose 6-phosphate
-
649729
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial
-
recombinant FLAG-tagged wild-type enzyme and mutants Y209C and T16R from COS-1 cells, removal of the tag
the phosphate-enzyme intermediate
-
the phosphate-enzyme-beta intermediate
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloning of two principal constituents: the catalytic subunit and D-glucose 6-phosphate translocase, expression studies in COS cells
-
enzyme catalytic subunit and D-glucose 6-phosphate transporter component
-
enzyme isoform of brain: G6PC3
expressed in COS-1 cells
-
expressed in HEK-293 cells and Hep-G2 cells
-
expressed in Hep-G2, HeLa, and CV1 cells
-
expression of FLAG-tagged wild-type and mutant enzymes in COS-1 cells, the FLAG-tag reduces the activity of the recombinant wild-type enzyme compared to the non-tagged wild-type enzyme; expression of FLAG-tagged wild-type enzyme and mutants Y209C and T16R in COS-1 cells, very low expression level of mutant enzymes
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of hepatic glucose-6-phosphatase-alpha is down-regulated in patients With hepatic steatosis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nordlie, R.C.; Sukalski, K.A.
Multifunctional glucose 6-phosphatase: a critical review
The Enzymes of Biological Membranes, 2nd Ed. (Martonosi, A. V. , ed. ), Plenum, New York
2
349-398
1985
Bos taurus, Cavia porcellus, Cricetulus griseus, Cyprinus carpio, Dictyostelium discoideum, Felis catus, Frog, Gallus gallus, Homo sapiens, Lampetra ayresii, Mus musculus, Oncorhynchus mykiss, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, salamander, Vicugna pacos
-
Manually annotated by BRENDA team
Suzuki, S.; Toyota, T.; Suzuki, H.; Goto, Y.
Partial purification from human mononuclear cells and placental plasma membranes of an insulin mediator which stimulates pyruvate dehydrogenase and suppresses glucose-6-phosphatase
Arch. Biochem. Biophys.
235
418-426
1984
Homo sapiens
Manually annotated by BRENDA team
Reczek, P.R.; Villee, C.A.
A purification of microsomal glucose-6-phosphatase from human tissue
Biochem. Biophys. Res. Commun.
107
1158-1165
1982
Homo sapiens
Manually annotated by BRENDA team
Nordlie, R.C.; Jorgenson, R.A.
Glucose-6-phosphatase
The Enzymes of Biological Membranes (Martonosi, A. V. , ed. ) Plenum, New York
2
465-491
1976
Anas platyrhynchos, Bos taurus, Canis lupus familiaris, Cervidae, Chondrichthyes, Columba livia, Cottus gobio, Felis catus, Gallus gallus, Homo sapiens, Mus musculus, Necturus maculosus, Oryctolagus cuniculus, Ovis aries, Rana catesbeiana, Rana sp., Rattus norvegicus, Thamnophis sirtalis, Trochilidae, Turtle
-
Manually annotated by BRENDA team
Nordlie, R.C.
Metabolic regulation by multifunctional glucose-6-phosphatase
Curr. Top. Cell. Regul.
8
33-117
1974
Anas platyrhynchos, Canis lupus familiaris, Cavia porcellus, Cervidae, Chondrichthyes, Columba livia, Felis catus, Gallus gallus, Homo sapiens, Mus musculus, Necturus maculosus, Oryctolagus cuniculus, Ovis aries, Rana catesbeiana, Rana sp., Rattus norvegicus, Thamnophis sirtalis, Trochilidae, Turtle
Manually annotated by BRENDA team
Nordlie, R.C.
Glucose-6-phosphatase, hydrolytic and synthetic activities
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
543-610
1971
Anas platyrhynchos, Astacoidea, Bos taurus, Canis lupus familiaris, Cavia porcellus, Columba livia, Equus caballus, Felis catus, Frog, Gallus gallus, Homo sapiens, Lampetra sp., Marmota sp., Mesocricetus auratus, Mus musculus, Necturus maculosus, Oryctolagus cuniculus, Ovis aries, Platyrrhini, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Van Schaftingen, E.; Gerin, I.
The glucose-6-phosphatase system
Biochem. J.
362
513-532
2002
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Foster, J.D.; Nordlie, R.C.
The biochemistry and molecular biology of the glucose-6-phosphatase system
Exp. Biol. Med.
227
601-608
2002
Homo sapiens
Manually annotated by BRENDA team
Guionie, O.; Clottes, E.; Stafford, K.; Burchell, A.
Identification and characterisation of a new human glucose-6-phosphatase isoform
FEBS Lett.
551
159-164
2003
Homo sapiens, Homo sapiens (Q9BUM1), Rattus norvegicus
Manually annotated by BRENDA team
Ghosh, A.; Shieh, J.J.; Pan, C.J.; Sun, M.S.; Chou, J.Y.
The Catalytic Center of Glucose-6-phosphatase
J. Biol. Chem.
277
32837-32842
2002
Homo sapiens
Manually annotated by BRENDA team
Shieh, J.J.; Terzioglu, M.; Hiraiwa, H.; Marsh, J.; Pan, C.J.; Chen, L.Y.; Chou, J.Y.
The molecular basis of glycogen storage disease type 1a: structure and function analysis of mutations in glucose-6-phosphatase
J. Biol. Chem.
277
5047-5053
2002
Homo sapiens
Manually annotated by BRENDA team
Ghosh, A.; Shieh, J.J.; Pan, C.J.; Chou, J.Y.
Histidine 167 is the phosphate acceptor in glucose-6-phosphatase-b forming a phosphohistidine enzyme intermediate during catalysis
J. Biol. Chem.
279
12479-12483
2004
Homo sapiens
Manually annotated by BRENDA team
Angaroni, C.J.; de Kremer, R.D.; Argarana, C.E.; Paschini-Capra, A.E.; Giner-Ayala, A.N.; Pezza, R.J.; Pan, C.J.; Chou, J.Y.
Glycogen storage disease type Ia in Argentina: two novel glucose-6-phosphatase mutations affecting protein stability
Mol. Genet. Metab.
83
276-279
2004
Homo sapiens, Homo sapiens (P35575)
Manually annotated by BRENDA team
Yang, J.; Danke, N.A.; Berger, D.; Reichstetter, S.; Reijonen, H.; Greenbaum, C.; Pihoker, C.; James, E.A.; Kwok, W.W.
Islet-specific glucose-6-phosphatase catalytic subunit-related protein-reactive CD4+ T cells in human subjects
J. Immunol.
176
2781-2789
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, S.; Pan, C.; Nandigama, K.; Mansfield, B.C.; Ambudkar, S.V.; Chou, J.Y.
The glucose-6-phosphate transporter is a phosphate-linked antiporter deficient in glycogen storage disease type Ib and Ic
FASEB J.
22
2206-2213
2008
Homo sapiens (P35575)
Manually annotated by BRENDA team
Kuo, M.; Zilberfarb, V.; Gangneux, N.; Christeff, N.; Issad, T.
O-glycosylation of FoxO1 increases its transcriptional activity towards the glucose 6-phosphatase gene
FEBS Lett.
582
829-834
2008
Homo sapiens
Manually annotated by BRENDA team
Chou, J.Y.; Mansfield, B.C.
Mutations in the glucose-6-phosphatase-alpha (G6PC) gene that cause type Ia glycogen storage disease
Hum. Mutat.
29
921-930
2008
Homo sapiens, Homo sapiens (P35575)
Manually annotated by BRENDA team
Hirota, K.; Sakamaki, J.; Ishida, J.; Shimamoto, Y.; Nishihara, S.; Kodama, N.; Ohta, K.; Yamamoto, M.; Tanimoto, K.; Fukamizu, A.
A combination of HNF-4 and Foxo1 is required for reciprocal transcriptional regulation of glucokinase and glucose-6-phosphatase genes in response to fasting and feeding
J. Biol. Chem.
283
32432-32441
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chen, W.M.; Erdos, M.R.; Jackson, A.U.; Saxena, R.; Sanna, S.; Silver, K.D.; Timpson, N.J.; Hansen, T.; Orru, M.; Grazia Piras, M.; Bonnycastle, L.L.; Willer, C.J.; Lyssenko, V.; Shen, H.; Kuusisto, J.; Ebrahim, S.; Sestu, N.; Duren, W.L.; Spada, M.C.; Stringham, H.M.; Scott, L.J.; Olla, N.; Swift, A.J.; Najjar, S.; Mitchell, B.D.; Lawlor, D.A.; Smith, G.D.; Ben-Shlomo, Y.; Andersen, G.; Borch-Johnsen, K.; Jørgensen, T.; Saramies, J.; Valle, T.T.; Buchanan, T.A.; Shuldiner, A.R.; Lakatta, E.; Bergman, R.N.; Uda, M.; Tuomilehto, J.; Pedersen, O.; Cao, A.; Groop, L.; Mohlke, K.L.; Laakso, M.; Schlessinger, D.; Collins, F.S.; Altshuler, D.; Abecasis, G.R.; Boehnke, M.; Scuteri, A.; Watanabe, R.M.
Variations in the G6PC2/ABCB11 genomic region are associated with fasting glucose levels
J. Clin. Invest.
118
2620-2628
2008
Homo sapiens (Q9NQR9)
Manually annotated by BRENDA team
Bouatia-Naji, N.; Rocheleau, G.; Van Lommel, L.; Lemaire, K.; Schuit, F.; Cavalcanti-Proenca, C.; Marchand, M.; Hartikainen, A.L.; Sovio, U.; De Graeve, F.; Rung, J.; Vaxillaire, M.; Tichet, J.; Marre, M.; Balkau, B.; Weill, J.; Elliott, P.; Jarvelin, M.R.; Meyre, D.; Polychronakos, C.; Dina, C.; Sladek, R.; Froguel, P.
A polymorphism within the G6PC2 gene is associated with fasting plasma glucose levels
Science
320
1085-1088
2008
Homo sapiens
Manually annotated by BRENDA team
Henry-Vitrac, C.; Ibarra, A.; Roller, M.; Merillon, J.M.; Vitrac, X.
Contribution of chlorogenic acids to the inhibition of human hepatic glucose-6-phosphatase activity in vitro by Svetol, a standardized decaffeinated green coffee extract
J. Agric. Food Chem.
58
4141-4144
2010
Homo sapiens
Manually annotated by BRENDA team
Hutton, J.C.; OBrien, R.M.
Glucose-6-phosphatase catalytic subunit gene family
J. Biol. Chem.
284
29241-29245
2009
Homo sapiens
Manually annotated by BRENDA team
Hayee, B.; Antonopoulos, A.; Murphy, E.J.; Rahman, F.Z.; Sewell, G.; Smith, B.N.; McCartney, S.; Furman, M.; Hall, G.; Bloom, S.L.; Haslam, S.M.; Morris, H.R.; Boztug, K.; Klein, C.; Winchester, B.; Pick, E.; Linch, D.C.; Gale, R.E.; Smith, A.M.; Dell, A.; Segal, A.W.
G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction
Glycobiology
21
914-924
2011
Homo sapiens
Manually annotated by BRENDA team
Konopelska, S.; Kienitz, T.; Quinkler, M.
Downregulation of Hepatic Glucose-6-Phosphatase-alpha in Patients With Hepatic Steatosis
Obesity (Silver Spring)
19
2322-2326
2011
Homo sapiens
Manually annotated by BRENDA team
Abbadi, S.; Rodarte, J.J.; Abutaleb, A.; Lavell, E.; Smith, C.L.; Ruff, W.; Schiller, J.; Olivi, A.; Levchenko, A.; Guerrero-Cazares, H.; Quinones-Hinojosa, A.
Glucose-6-phosphatase is a key metabolic regulator of glioblastoma invasion
Mol. Cancer Res.
12
1547-1559
2014
Homo sapiens
Manually annotated by BRENDA team
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