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EC Tree
IUBMB Commentscf. EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae
Synonyms
fructose-2,6-bisphosphate 6-phosphatase, fructose-2,6-bisphosphate 6-phosphohydrolase,
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fructose 2,6-bisphosphate-6-phosphohydrolase
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fructose-2,6-bisphosphate 6-phosphohydrolase
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phosphatase, fructose 2,6-diphosphate 6-
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beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructofuranose 2-phosphate + phosphate
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hydrolysis of phosphoric ester
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beta-D-fructose-2,6-bisphosphate 6-phosphohydrolase
cf. EC 3.1.3.46 fructose-2,6-bisphosphate 2-phosphatase.
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
4-nitrophenyl phosphate + H2O

4-nitrophenol + phosphate
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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D-fructose 2,6-bisphosphate + H2O

D-fructose 2-phosphate + phosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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synonym: furanose
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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participates in maintenance of a steady state level of fructose 2,6-bisphosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
D-fructose 2,6-bisphosphate + H2O

D-fructose 2-phosphate + phosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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participates in maintenance of a steady state level of fructose 2,6-bisphosphate
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D-fructose 2,6-bisphosphate + H2O
D-fructose 2-phosphate + phosphate
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Cu2+
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dimer contains 1.3 mol copper per mol of subunit
Mg2+
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required, half-maximal activity at 0.15 mM
Zn2+
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dimer contains 1.5 mol zinc per mol of subunit
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D-Fructose 2-phosphate
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50% inhibition at 0.008 mM
D-fructose 6-phosphate
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50% inhibition at 0.08 mM
D-glucose 6-phosphate
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50% inhibition at 0.045 mM
diphosphate
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50% inhibition at 0.3 mM
Neocuproine
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i.e. 2,9-dimethyl-1,10-phenanthroline, 0.1 mM Zn2+ stabilizes the activity
phosphate
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50% inhibition at 0.9 mM
additional information
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no inhibitor: fructose
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0.006 - 0.079
D-fructose 2,6-bisphosphate
0.006
D-fructose 2,6-bisphosphate

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0.0072
D-fructose 2,6-bisphosphate
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pH 6.0
0.079
D-fructose 2,6-bisphosphate
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pH 7.0
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additional information

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additional information
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6
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with D-fructose 2,6-bisphosphate as substrate
6 - 6.5
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D-fructose 2,6-bisphosphate
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above, 4-nitrophenyl phosphate
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above, 4-nitrophenyl phosphate
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4 - 7.5
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pH 4: about 25% of activity maximum, pH 7.5: about 20% of activity maximum, fructose 2,6-bisphosphate
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brenda
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brenda
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brenda
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brenda
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PPB_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
566
1
63004
Swiss-Prot
other Location (Reliability: 4)
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60000
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2 * 60000, SDS-PAGE
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dimer
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2 * 60000, SDS-PAGE
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glycoprotein

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30
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pH 7.7, about 60% loss of activity after 15 min, fructose-2,6-bisphosphate 6-phosphohydrolase activity
40
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pH 7.0, 5 min, stable, fructose-2,6-bisphosphate 6-phosphohydrolase activity
50
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pH 7.0, 5 min, about 30% loss of activity, fructose-2,6-bisphosphate 6-phosphohydrolase activity
60
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pH 7.0, 5 min, about 70% loss of activity, fructose-2,6-bisphosphate 6-phosphohydrolase activity
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Purwin, C.; Laux, M.; Holzer, H.
Fructose 2-phosphate, an intermediate of the dephosphorylation of fructose 2,6-bisphosphate with a purified yeast enzyme
Eur. J. Biochem.
164
27-30
1987
Saccharomyces cerevisiae
brenda
Purwin, C.; Laux, M.; Holzer, H.
Fructofuranose 2-phosphate is the product of dephosphorylation of fructose 2,6-bisphosphate
Eur. J. Biochem.
165
543-545
1987
Saccharomyces cerevisiae
brenda
Plankert, U.; Purwin, C.; Holzer, H.
Yeast fructose-2,6-bisphosphate 6-phosphatase is encoded by PHO8, the gene for nonspecific repressible alkaline phosphatase
Eur. J. Biochem.
196
191-196
1991
Saccharomyces cerevisiae, Saccharomyces cerevisiae M1
brenda
Plankert, U.; Purwin, C.; Holzer, H.
Characterization of yeast fructose-2,6-bisphosphate 6-phosphatase
FEBS Lett.
239
69-72
1988
Saccharomyces cerevisiae
brenda
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