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Information on EC 3.1.3.68 - 2-deoxyglucose-6-phosphatase
for references in articles please use BRENDA:EC3.1.3.68
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.68 2-deoxyglucose-6-phosphatase
IUBMB Comments
Also active towards fructose 1-phosphate
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 3.1.3.68
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catabolite
- phosphatases
- analysis
showSynonyms
2-deoxyglucose-6-phosphate phosphatase, 2-dog-6p phosphatase, 2-deoxyglucose-6-phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-Deoxyglucose 6-phosphate phosphatase
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2-Deoxyglucose-6-phosphate phosphatase
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2-DOG-6P phosphatase
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GenBank AE000318-derived protein GI 1788630
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GenBank D90861-derived protein GI 1799667
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Phosphatase, 2-deoxyglucose 6-
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Phosphatase, 2-deoxyglucose 6- (Escherichia coli strain K-12 Kohara clone 405 gene DOG1)
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Phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae clone pGEMT-DOGR1)
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Phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR1 isoform)
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Phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR1)
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Phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR2 isoform)
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Protein (Escherichia coli strain K12-MG1655 gene b2293)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose + phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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PATHWAY SOURCE
PATHWAYS
MetaCyc
2-deoxy-D-glucose 6-phosphate degradation
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SYSTEMATIC NAME
IUBMB Comments
2-deoxy-D-glucose-6-phosphate phosphohydrolase
Also active towards fructose 1-phosphate
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CAS REGISTRY NUMBER
COMMENTARY
159036-75-6
phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR1) /phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae clone pGEMT-DOGR1) /phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR1 isoform)
172400-89-4
phosphatase, 2-deoxyglucose 6- (Saccharomyces cerevisiae gene DOGR2 isoform)
1923393-20-7
phosphatase, 2-deoxyglucose 6- (Escherichia coli strain K-12 Kohara clone 405 gene DOG1) /genBank AE000318-derived protein GI 1788630 / /genBank D90861-derived protein GI 1799667 /protein (Escherichia coli strain K12-MG1655 gene b2293)
65187-56-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
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Substrates: -
Products: -
Products: -
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2-Deoxyribose 5-phosphate + H2O
2-Deoxyribose + phosphate
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Substrates: isoenzyme DogR1p: at 21% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 1% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Arabinose 5-phosphate + H2O
Arabinose + phosphate
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Substrates: isoenzyme DogR1p: at 6% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 6% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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D-fructose 6-phosphate + H2O
D-fructose + phosphate
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Substrates: isoenzyme DogR1p: at 2% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 17% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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D-ribulose 5-phosphate + H2O
D-ribulose + phosphate
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Substrates: -
Products: -
Products: -
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D-xylulose 5-phosphate + H2O
D-xylulose + phosphate
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Substrates: -
Products: -
Products: -
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Glucose 6-phosphate + H2O
Glucose + phosphate
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Substrates: isoenzyme DogR1p: at 20% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 30% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Ribulose 5-phosphate + H2O
Ribulose + phosphate
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Substrates: isoenzyme DogR1p: at 7% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 1% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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2-Deoxy-D-glucose 6-phosphate + H2O
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Substrates: the expression of the enzyme is increased by the presence of 2-deoxyglucose and is constant along the growth curve
Products: -
Products: -
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2-Deoxy-D-glucose 6-phosphate + H2O
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Substrates: the enzyme may be involved in inhibiting the process of catabolite repression mediated by 2-deoxyglucose
Products: -
Products: -
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D-ribose 5-phosphate + H2O
D-ribose + phosphate
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Substrates: -
Products: -
Products: -
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D-ribose 5-phosphate + H2O
D-ribose + phosphate
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Substrates: isoenzyme DogR1p: at 42% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 13% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Fructose 1-phosphate + H2O
Fructose + phosphate
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Substrates: with 80% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Fructose 1-phosphate + H2O
Fructose + phosphate
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Substrates: isoenzyme DogR1p: at 12% of the activity with 2-deoxy-D-glucose 6-phosphate, isoenzyme DogR2p: at 106% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Fructose 1-phosphate + H2O
Fructose + phosphate
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Substrates: with 80% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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Fructose 1-phosphate + H2O
Fructose + phosphate
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Substrates: with 80% of the activity with 2-deoxy-D-glucose 6-phosphate
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-Deoxy-D-glucose 6-phosphate + H2O
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Substrates: the expression of the enzyme is increased by the presence of 2-deoxyglucose and is constant along the growth curve
Products: -
Products: -
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2-Deoxy-D-glucose 6-phosphate + H2O
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Substrates: the enzyme may be involved in inhibiting the process of catabolite repression mediated by 2-deoxyglucose
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
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can replace Mg2+ in activation, with less than 15% of the efficiency
Mg2+
Mn2+
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can replace Mg2+ in activation, with less than 15% of the efficiency
Zn2+
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can replace Mg2+ in activation, with less than 15% of the efficiency
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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2-deoxy-glucose 6-phosphate (100%), D-ribulose 5-phosphate (7%), D-ribose 5-phosphate (42%), D-xylulose 5-phosphate (15%)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the enzyme is also present in wild type yeast, although its level is ten to twenty times lower than those found in the mutant
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brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (292 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of DOG1 in Saccharomyces cerevisiae transketolase-deficient strain H1520 containing the integrated xylitol dehydrogenase-encoding gene (XYL2) gene increases the excretion of ribitol (by 1.6fold) and D-ribose (by 3.8fold) compared to the strain lacking DOG1
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
use of gene as a selectable marker gene to produce transgenic plants by Agrobacterium tumefaciens-mediated transfection of oil palm and regeneration of resistant tissues into whole plantlets on various regeneration media containing the same concentration of 2-deoxyglucose-6-phosphate. A transformation efficiency of about 1.0% is obtained
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Randez-Gil, F.; Blasco, A.; Prieto, J.A.; Sanz, P.
DOGR1 and DOGR2: two genes from Saccharomyces cerevisiae that confer 2-deoxyglucose resistance when overexpressed
Yeast
11
1233-1240
1995
Saccharomyces cerevisiae
brenda
Randez-Gil, F.; Prieto, J.A.; Sanz, P.
The expression of a specific 2-deoxyglucose-6-P phosphatase prevents catabolite repression mediated by 2-deoxyglucose in yeast
Curr. Genet.
28
101-107
1995
Saccharomyces cerevisiae
brenda
Sanz, P.; Randez-Gil, F.; Prieto, J.A.
Molecular characterization of a gene that confers 2-deoxyglucose resistance in yeast
Yeast
10
1195-1202
1994
Saccharomyces cerevisiae
brenda
Martin, M.; Heredia, C.F.
Characterization of a phosphatase specific for 2-deoxyglucose-6-phosphate in a yeast mutant
FEBS Lett.
83
245-248
1977
Saccharomyces cerevisiae, Saccharomyces cerevisiae 10a12-13, Saccharomyces cerevisiae PM-II
brenda
Toivari, M.H.; Ruohonen, L.; Miasnikov, A.N.; Richard, P.; Penttila, M.
Metabolic engineering of Saccharomyces cerevisiae for conversion of D-glucose to xylitol and other five-carbon sugars and sugar alcohols
Appl. Environ. Microbiol.
73
5471-5476
2007
Saccharomyces cerevisiae
brenda
Izawati, A.M.; Masani, M.Y.; Ismanizan, I.; Parveez, G.K.
Evaluation on the effectiveness of 2-deoxyglucose-6-phosphate phosphatase (DOG(R)1) gene as a selectable marker for oil palm (Elaeis guineensis Jacq.) embryogenic calli transformation mediated by Agrobacterium tumefaciens
Front. Plant Sci.
6
727
2015
Saccharomyces cerevisiae (P38774)
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.3.68)
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