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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30298

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.11 fructose-bisphosphatase
IUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O30298
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Synonyms
fructose-1,6-bisphosphatase, fructose 1,6-bisphosphatase, fructose bisphosphatase, fructose-bisphosphatase, fructose 1,6-diphosphatase, fbp-1, fructose diphosphatase, fru-1,6-p2ase, cytosolic fbpase, cfbp1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CY-F1
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-
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D-fructose 1,6-diphosphatase
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-
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D-fructose-1,6-bisphosphatase
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-
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D-fructose-1,6-bisphosphate 1-phosphohydrolase
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D-fructose-1,6-bisphosphate phosphatase
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-
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FBPase
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Fru-1,6-P2ase
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fructose 1,6-bisphosphatase
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-
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fructose 1,6-bisphosphate 1-phosphatase
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fructose 1,6-bisphosphate phosphatase
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-
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fructose 1,6-diphosphatase
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-
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fructose 1,6-diphosphate phosphatase
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fructose bisphosphate phosphatase
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fructose diphosphatase
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fructose diphosphate phosphatase
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hexose bisphosphatase
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-
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hexose diphosphatase
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-
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hexosediphosphatase
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RAE-30
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate 1-phosphohydrolase
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-52-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
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-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
show the reaction diagram
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-
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.15
D-fructose 1,6-bisphosphate
additional information
additional information
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enzyme shows unusual temperature dependence for its main substrate di-myo-inositol 1,1’-phosphate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
212
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56.8
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
290
Li+
Archaeoglobus fulgidus
pH 8.0, 85°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by vapor diffusion using hanging drops of 0.005 ml. The apoenzyme is crystallized in either 0.2 M ammonium nitrate and 30% PEG 3350 or 0.2 M dihydrogen ammonium phosphate and 30% PEG 3350
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.K.; Morgan, A.; Stieglitz, K.; Stec, B.; Thompson, B.; Miller, S.J.; Roberts, M.F.
The temperature dependence of the inositol monophosphatase Km correlates with accumulation of di-myo-inositol 1,1'-phosphate in Archaeoglobus fulgidus
Biochemistry
45
3307-3314
2006
Archaeoglobus fulgidus
Manually annotated by BRENDA team
Stieglitz, K.A.; Johnson, K.A.; Yang, H.; Roberts, M.F.; Seaton, B.A.; Head, J.F.; Stec, B.
Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop
J. Biol. Chem.
277
22863-22874
2002
Archaeoglobus fulgidus (O30298)
Manually annotated by BRENDA team
Kawai, S.; Murata, K.
Structure and function of NAD kinase and NADP phosphatase key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
Biosci. Biotechnol. Biochem.
72
919-930
2008
Archaeoglobus fulgidus (O30298), Methanocaldococcus jannaschii (Q57573), Methanocaldococcus jannaschii (Q58327), Archaeoglobus fulgidus ATCC 49558 (O30298), Methanocaldococcus jannaschii ATCC 43067 (Q57573), Methanocaldococcus jannaschii ATCC 43067 (Q58327)
Manually annotated by BRENDA team