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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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EC Tree
     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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Homo sapiens
UNIPROT: Q9NQR9
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glucose-6-phosphatase, g6pase, glucose 6-phosphatase, g-6-pase, g6pc2, islet-specific glucose-6-phosphatase catalytic subunit-related protein, g6pc1, g6pase-alpha, glucose-6-phosphatase-alpha, g6pase-beta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glucose-6-phosphatase catalytic subunit 2
-
islet-specific glucose-6-phosphatase-related protein
-
G-6-Pase
-
-
-
-
G6Pase
G6Pase-alpha
-
G6Pase-beta
-
-
G6Pc1
G6PC2
-
-
glucose 6-phosphate phosphatase
-
-
-
-
glucose 6-phosphate phosphohydrolase
-
-
-
-
glucose-6-phosphatase
glucose-6-phosphatase catalytic subunit-related protein
-
-
glucose-6-phosphatase catalytic unit 2
-
-
glucose-6-phosphatase-alpha
glucose-6-phosphatase-beta
-
-
islet-specific glucose-6-phosphatase catalytic subunit-related protein
-
-
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
-
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
cAMP
enzyme activation by cAMP depends on protein kinase A
D-glucose
-
elevated concentration, D-glucose may play a direct role as a stimulator of enzyme expression
forskolin
forskolin treatment promotes a 70% stimulation of G6Pase activity. The increase in glucose-6-phosphate transporter activity is required for the stimulation of glucose-6-phosphatase activity by forskolin
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
136
recombinant non-tagged wild-type enzyme
6.58
-
enzyme from placenta
67.7
recombinant FLAG-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
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
physiological function
-
the enzyme is required for glucose uptake, ATP production, and Ca2+ uptake by the endoplasmic reticulum
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PC2_HUMAN
355
7
40580
Swiss-Prot
other Location (Reliability: 3)
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
?
-
x * 40000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
side-chain modification
-
enzyme is active as a phosphoprotein, dephosphorylation leads to inactivation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FoxO1 DNA binding domain in complex with the G6PC1 promoter, hanging drop vapor diffusion method, using 14-18% (v/v) PEG 8000, 100 mM ammonium sulfate, 20 mM magnesium chloride, 50 mM MES pH 5.6 and 10% (v/v) glycerol
-
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
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
T145A
the mutation does not affect the enzyme activity compared to the wild type
T145D
the mutation does not affect the enzyme activity compared to the wild type
T16A
site-directed mutagenesis, 74-78% reduced activity compared to the wild-type enzyme
V166A
the mutation leads to reduced levels of G6PC protein
W63R/G68R
the mutation leads to reduced levels of G6PC protein
Y209C
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 Escherichia coli BL21(DE3)-Rosetta2 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
-
the expression of the enzyme is significantly elevated, up to 11fold in Hep-G2 cells under starvation-induced autophagy condition compared to normal condition
-
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, Cyprinus carpio, Cavia porcellus, Gallus gallus, Cricetulus griseus, Oryctolagus cuniculus, Dictyostelium discoideum, Felis catus, Frog, Homo sapiens, Vicugna pacos, Lampetra ayresii, Platyrrhini, Mus musculus, Oncorhynchus mykiss, Rattus norvegicus, salamander
-
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, Gallus gallus, Columba livia, Cottus gobio, Oryctolagus cuniculus, Cervidae, Felis catus, Chondrichthyes, Ovis aries, Homo sapiens, Trochilidae, Mus musculus, Necturus maculosus, Lithobates catesbeianus, Rana sp., Rattus norvegicus, Thamnophis sirtalis, 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, Gallus gallus, Columba livia, Oryctolagus cuniculus, Cervidae, Felis catus, Chondrichthyes, Ovis aries, Homo sapiens, Trochilidae, Mus musculus, Necturus maculosus, Lithobates catesbeianus, Rana sp., Rattus norvegicus, Thamnophis sirtalis, 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, Bos taurus, Canis lupus familiaris, Cavia porcellus, Gallus gallus, Columba livia, Astacoidea, Oryctolagus cuniculus, Equus caballus, Felis catus, Frog, Ovis aries, Homo sapiens, Lampetra sp., Marmota sp., Mesocricetus auratus, Platyrrhini, Mus musculus, Necturus maculosus, 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
Rattus norvegicus, Homo sapiens (Q9BUM1), Homo sapiens
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 (P35575), Homo sapiens
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 (P35575), Homo sapiens
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.; Jrgensen, 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
Jeon, J.Y.; Lee, H.; Park, J.; Lee, M.; Park, S.W.; Kim, J.S.; Lee, M.; Cho, B.; Kim, K.; Choi, A.M.; Kim, C.K.; Yun, M.
The regulation of glucose-6-phosphatase and phosphoenolpyruvate carboxykinase by autophagy in low-glycolytic hepatocellular carcinoma cells
Biochem. Biophys. Res. Commun.
463
440-446
2015
Homo sapiens
Manually annotated by BRENDA team
Mueller, M.S.; Fouyssac, M.; Taylor, C.W.
Effective glucose uptake by human astrocytes requires its sequestration in the endoplasmic reticulum by glucose-6-phosphatase-beta
Curr. Biol.
28
3481-3486
2018
Homo sapiens
Manually annotated by BRENDA team
Soty, M.; Chilloux, J.; Delalande, F.; Zitoun, C.; Bertile, F.; Mithieux, G.; Gautier-Stein, A.
Post-translational regulation of the glucose-6-phosphatase complex by cyclic adenosine monophosphate is a crucial determinant of endogenous glucose production and is controlled by the glucose-6-phosphate transporter
J. Proteome Res.
15
1342-1349
2016
Homo sapiens (P35575)
Manually annotated by BRENDA team
Singh, P.; Han, E.H.; Endrizzi, J.A.; OBrien, R.M.; Chi, Y.I.
Crystal structures reveal a new and novel FoxO1 binding site within the human glucose-6-phosphatase catalytic subunit 1 gene promoter
J. Struct. Biol.
198
54-64
2017
Homo sapiens
Manually annotated by BRENDA team