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Information on EC 3.1.3.46 - fructose-2,6-bisphosphate 2-phosphatase and Organism(s) Bos taurus and UniProt Accession P49872
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EC Tree
3.1.3.46 fructose-2,6-bisphosphate 2-phosphataseIUBMB Comments
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
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Word Map
- 3.1.3.46
- fructose-1,6-bisphosphatase
-
gluconeogenesis
-
gluconeogenic
- amp
- 6-phosphate
-
1,6-bisphosphatase
-
tp53-induced
- phosphoenolpyruvate
- isozyme
- chloroplast
- endothelial
- glycogen
- pentose
- 6-phosphofructo-1-kinase
- hepatocytes
-
carboxykinase
- fructose-6-phosphate
-
hypoxia-inducible
- glucokinase
-
camp-dependent
-
warburg
- pepck
-
3.1.3.11
-
glucose-induced
- g6pase
- spinach
- hk2
-
fructose-1
- hypoglycemia
- glucose-6-phosphatase
- hexokinase
-
fru-6-p
-
glycogenolysis
-
calvin
-
p53-inducible
-
anaphase-promoting
- phosphofructokinase-1
- phosphoenzyme
-
fructose-6-p
- molecular biology
- medicine
- pharmacology
- agriculture
-
pentose-phosphate
-
z-line
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
fbpase, pfkfb3, tigar, pfk-2, pfkfb4, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, fructose-2,6-bisphosphatase, pfkfb2, pfk-2/fbpase-2, f-2,6-p2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-fructose-2,6-bisphosphatase
-
-
-
-
fructose-2,6-bisphosphatase
fructose-2,6-diphosphatase
-
-
-
-
phosphatase, fructose 2,6-di-
-
-
-
-
additional information
fructose-2,6-bisphosphatase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
bifunctional enzyme: 6-phosphofructo-2-kinase-fructose-2,6-bisphosphatase
-
beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
FBPase performs a reaction following a classical ping pong mechanism with formation of a phosphoryl-enzyme intermediate on a histidine residue located in an Arg-His-Gly triad, catalytic site structure, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-fructose-2,6-bisphosphate 2-phosphohydrolase
The enzyme copurifies with EC 2.7.1.105 6-phosphofructo-2-kinase. (cf. EC 3.1.3.54 fructose-2,6-bisphosphate 6-phosphatase).
CAS REGISTRY NUMBER
COMMENTARY
81611-75-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB1
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB2
-
-
?
beta-D-fructose 2,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
metabolic regulation of isozyme PFKFB3
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Protein kinase C
-
phosphorylation requires phosphatidyl serine, Ca2+ and diolein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
tissue-specific expression of the different isozymes, overview
additional information
tissue-specific expression of the different isozymes, overview
additional information
tissue-specific expression of the different isozymes, overview
additional information
tissue-specific expression of the different isozymes, overview
additional information
tissue-specific expression of the different isozymes, overview
additional information
tissue-specific expression of the different isozymes, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F261_BOVIN
471
0
54657
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
additional information
domain organization of the bifunctional enzyme, head-to-head structure of the two subunits of the bifunctional enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 1.8 A resolution. Citrate cocrystallizes in the 2-kinase domain, occupying the fructose-6-phosphate binding-site and extending into the gamma-phosphate binding pocket of ATP. In complex with ADP, ADP mimicks the catalytic binding mode of ATP
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, transcriptional control of isozymes, overview
phylogenetic analysis, transcriptional control of isozymes, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taniyama, M.; Kitamura, K.; Thomas, H; Lawson, J.W.R.; Uyeda, K.
Isozymes of fructose 6-phosphate, 2-kinase:fructose-2,6-bisphosphatase in rat and bovine heart, liver, and skeletal muscle
Biochem. Biophys. Res. Commun.
157
949-954
1988
Bos taurus, Rattus norvegicus
Pilkis, S.J.; Claus, T.H.; Kountz, P.D.; El-Maghrabi, M.R.
Enzymes of the fructose 6-phosphate-fructose 1,6-bisphosphate substrate cycle
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
18
3-46
1987
Bos taurus, Rattus norvegicus
-
Kitamura, K.; Uyeda, K.; Hartman, F.C.; Kangawa, K.; Matsuo, H.
Catalytic site of rat liver and bovine heart fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase
J. Biol. Chem.
264
6344-6348
1989
Bos taurus, Rattus norvegicus
Sakata, J.; Abe, Y.; Uyeda, K.
Molecular cloning of the DNA and expression and characterization of rat testes fructose-6-phosphate,2-kinase: fructose-2,6-bisphosphatase
J. Biol. Chem.
266
15764-15770
1991
Bos taurus
Sakata, J.; Uyeda, K.
Characterization of two isozymic forms of heart fructose 6-phosphate, 2-kinase:fructose 2,6-bisphosphatase
Biochem. Biophys. Res. Commun.
180
470-474
1991
Bos taurus
Rider, M.H.; Bertrand, L.; Vertommen, D.; Michels, P.A.; Rousseau, G.G.; Hue, L.
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis
Biochem. J.
381
561-579
2004
Arabidopsis thaliana (Q9MB58), Bos taurus (P26285), Bos taurus (P49872), Bos taurus (Q28901), Desulfovibrio desulfuricans, Drosophila melanogaster (Q9VWH7), Homo sapiens (O60825), Homo sapiens (P16118), Homo sapiens (Q16875), Homo sapiens (Q16877), Leishmania major, Mus musculus (P70265), Mus musculus (Q9ESY2), Rattus norvegicus (O35552), Rattus norvegicus (P07953), Rattus norvegicus (P25114), Rattus norvegicus (Q9JJH5), Schizosaccharomyces pombe
Crochet, R.; Kim, J.; Lee, H.; Yim, Y.; Kim, S.; Neau, D.; Lee, Y.
Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding
Proteins
85
117-124
2017
Homo sapiens (O60825), Homo sapiens, Bos taurus (P26285), Bos taurus
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