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Information on EC 3.1.3.11 - fructose-bisphosphatase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WN21
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3.1.3.11 fructose-bisphosphataseIUBMB Comments
The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
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Word Map
- 3.1.3.11
- fbpases
-
gluconeogenesis
-
gluconeogenic
- amp
- chloroplast
- phosphoenolpyruvate
-
carboxykinase
- glycogen
- glucose-6-phosphatase
-
phosphofructokinase
- hexokinase
- 2,6-bisphosphate
- spinach
- malate
- thioredoxins
- carboxylase
- starch
- co2
- glucokinase
- phosphorylase
-
6-phosphatase
- fructose-2,6-bisphosphate
- pepck
- trx
- fructose-6-phosphate
- 3-phosphoglycerate
-
nadp-malate
- oleracea
- dihydroxyacetone
- g6pase
- ribulose
- ribulose-1,5-bisphosphate
- triose
-
calvin
- glucagon
- rubisco
-
sucrose-phosphate
-
light-activated
-
amp-dependent
-
antihyperglycemic
- phosphoribulokinase
- 6-phosphofructo-1-kinase
-
calvin-benson
-
monophosphatase
- rubp
- ribulose-5-phosphate
- biofuel production
- synthesis
- medicine
- biotechnology
- molecular biology
- drug development
- diagnostics
-
4.1.1.39
-
t-states
-
2.7.1.11
-
triose-phosphate
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
class II fructose-1,6-bisphosphatase
CY-F1
-
-
-
-
D-fructose 1,6-diphosphatase
-
-
-
-
D-fructose-1,6-bisphosphatase
-
-
-
-
D-fructose-1,6-bisphosphate 1-phosphohydrolase
-
-
-
-
D-fructose-1,6-bisphosphate phosphatase
-
-
-
-
FBPase
Fru-1,6-P2ase
-
-
-
-
fructose 1,6-bisphosphatase
-
-
-
-
fructose 1,6-bisphosphate 1-phosphatase
-
-
-
-
fructose 1,6-bisphosphate phosphatase
-
-
-
-
fructose 1,6-diphosphatase
-
-
-
-
fructose 1,6-diphosphate phosphatase
-
-
-
-
fructose bisphosphate phosphatase
-
-
-
-
fructose diphosphatase
-
-
-
-
fructose diphosphate phosphatase
-
-
-
-
hexose bisphosphatase
-
-
-
-
hexose diphosphatase
-
-
-
-
hexosediphosphatase
-
-
-
-
RAE-30
-
-
-
-
FBPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate
the proposed mechanism involves two metal ions near the cleavable phosphate: one to stabilize the negative charge on the leaving group and one to coordinate the nucleophilic water
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
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
9001-52-9
-
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
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
additional information
?
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
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
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the apoenzyme does not contain Mg2+ in the active site, instead Mg2+ is found in helices H8 and H9 in one chain, coordinated to Leu165 N, Gln164 N and Arg161 O and possibly stabilizing this loop. The fructose 6-phosphate-bound structures contain one magnesium ion in a position that is proposed to bind fructose 1,6-bisphosphate, coordinate the 1-phosphate and stabilize the transition state
additional information
the apoenzyme does not contain Mg2+ in the active site, instead Mg2+ is found in helices H8 and H9 in one chain, coordinated to Leu165 N, Gln164 N and Arg161 O and possibly stabilizing this loop. The fructose 6-phosphate-bound structures contain one magnesium ion in a position that is proposed to bind fructose 1,6-bisphosphate, coordinate the 1-phosphate and stabilize the transition state
additional information
-
the apoenzyme does not contain Mg2+ in the active site, instead Mg2+ is found in helices H8 and H9 in one chain, coordinated to Leu165 N, Gln164 N and Arg161 O and possibly stabilizing this loop. The fructose 6-phosphate-bound structures contain one magnesium ion in a position that is proposed to bind fructose 1,6-bisphosphate, coordinate the 1-phosphate and stabilize the transition state
additional information
-
the enzyme activity is dependent on bivalent metal ions, but Co2+, Ni2+, Cu2+, Zn2+, Fe2+ and Ca2+ show no significant activation of FBPase at any specific concentration
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
-
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
enzyme mutant T84S can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
0.0057
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.22
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
2.1
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
2-oxoglutarate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
2
citrate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.3
malate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.2
malonate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
6.4
oxaloacetate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.1
alpha-ketoglutarate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
2
citrate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3.3
malate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3.2
malonate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
6.4
oxaloacetate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
structural comparison of class I versus class II FBPases
malfunction
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
physiological function
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
metabolism
additional information
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
metabolism
-
fructose 1,6-bisphosphatase II is a key gluconeogenic enzyme
metabolism
-
fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
x * 36000, recombinant His-tagged enzyme, SDS-PAGE, x * 36612.5, recombinant His-tagged enzyme, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 36584, recombinant mutant T84A, mass spectrometry and sequence calculation, x * 36599, recombinant mutant T84S, mass spectrometry and sequence calculation
oligomer
-
x * 36000, recombinant His-tagged enzyme, SDS-PAGE, x * 36612.5, recombinant His-tagged enzyme, mass spectrometry
additional information
additional information
the constellation of amino-acid residues in the active site of FBPaseII from Mycobacterium tuberculosis (MtFBPaseII) is conserved and is analogous to that described previously for the Escherichia coli enzyme, structure analysis and comparisons, overview
additional information
the constellation of amino-acid residues in the active site of FBPaseII from Mycobacterium tuberculosis (MtFBPaseII) is conserved and is analogous to that described previously for the Escherichia coli enzyme, structure analysis and comparisons, overview
additional information
-
the constellation of amino-acid residues in the active site of FBPaseII from Mycobacterium tuberculosis (MtFBPaseII) is conserved and is analogous to that described previously for the Escherichia coli enzyme, structure analysis and comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type apoform and two active site mutants T84A and T84S in complex with D-fructose 1,6-bisphosphate or D-fructose 6-phosphate (F6P), hanging drop vapor diffusion method, mixing of protein and precipitant solution in a 1:1 ratio, the reservoir solution contains 1.0 M ammonium citrate tribasic, pH 7.0, and 1% PEG 3350, for the apoenzyme, and 2.4 M sodium malonate, pH 6.0, with 1 mM ligand, for the complexed mutant enzyme crystals, X-ray diffraction structure determination and analysis at 2.6 A, 2.3 A, and 2.2 A resolution, respectively, crystal structures of apo MtFBPaseII, the T84A MtFBPase-F6P complex and the T84S MtFBPase-F6P complex are solved by molecular replacement
hanging-drop vapor-diffusion method at 25°C, crystal structures of native enzyme (FBPaseII) at 2.6 A resolution and two active-site protein variants. The variants are complexed with the reaction product fructose 6-phosphate. Presence of a 222 tetramer
purified recombinant His-tagged enzyme, hanging-drop vapor-diffusion method, 0.001 ml of protein solution containing 10 mg/ml protein, is mixed with 0.001 ml of reservoir solution containing 1.8 M ammonium citrate tribasic, pH 7.0, and equilibratzion against 0.3 ml reservoir solution, 72 h to 2 weeks, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T84A
T84S
D40N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
D94N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
L71A
-
no loss of either of the activities, activity toward inositol is more resisitant to inhibition by calcium than wild-type
T84A
site-directed mutagenesis, catalytically inactive active-site mutant
T84A
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
T84A
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
T84S
site-directed mutagenesis, active-site mutant, the mutant shows reduced activity compared to wild-type. One Mg2+ ion is found in T84S MtFBPaseII, coordinated to a glycerol molecule and to Asp79, Asp82, and Glu208 near the cleaved 1-phosphate group of the substrate
T84S
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
T84S
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
-
purified recombinant His-tagged enzyme, 30 min, completely stable
40
40
-
purified recombinant His-tagged enzyme, 30 min, loss of 65% activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and desalting gel filtration
recombinant N-terminally His-tagged wild-type and mutant enzymes by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme 70.7fold from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene glpX, sequence comparisons of class II FBPases, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of N-terminally His-tagged wild-type and mutant enzymes
expression of the His-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
gene glpX, expression of functional N-terminally His-tagged enzyme in Escherichia coli strain BL21 (DE3), suncloning in Escherichia coli strain DH5alpha
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gu, X.; Chen, M.; Shen, H.; Jiang, X.; Huang, Y.; Wang, H.
Rv2131c gene product: an unconventional enzyme that is both inositol monophosphatase and fructose-1,6-bisphosphatase
Biochem. Biophys. Res. Commun.
339
897-904
2006
Mycobacterium tuberculosis
Movahedzadeh, F.; Rison, S.C.; Wheeler, P.R.; Kendall, S.L.; Larson, T.J.; Stoker, N.G.
The Mycobacterium tuberculosis Rv1099c gene encodes a GlpX-like class II fructose 1,6-bisphosphatase
Microbiology
150
3499-3505
2004
Mycobacterium tuberculosis (P9WN21), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WN21)
Gutka, H.J.; Franzblau, S.G.; Movahedzadeh, F.; Abad-Zapatero, C.
Crystallization and preliminary X-ray characterization of the glpX-encoded class II fructose-1,6-bisphosphatase from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
67
710-713
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Gutka, H.J.; Rukseree, K.; Wheeler, P.R.; Franzblau, S.G.; Movahedzadeh, F.
glpX gene of Mycobacterium tuberculosis: heterologous expression, purification, and enzymatic characterization of the encoded fructose 1,6-bisphosphatase II
Appl. Biochem. Biotechnol.
164
1376-1389
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Wolf, N.; Gutka, H.; Movahedzadeh, F.; Abad-Zapatero, C.
Structures of the mycobacterium tuberculosis glpx protein (Class II fructose-1,6-bisphosphatase) Implications for the active oligomeric state, catalytic mechanism and citrate inhibition
Acta Crystallogr. Sect. D
74
321-331
2018
Mycobacterium tuberculosis (P9WN20), Mycobacterium tuberculosis (P9WN21), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WN21)
Bondoc, J.; Wolf, N.; Ndichuck, M.; Abad-Zapatero, C.; Movahedzadeh, F.
Mutagenesis of threonine to serine in the active site of Mycobacterium tuberculosis fructose-1,6-bisphosphatase (Class II) retains partial enzyme activity
Biotechnol. Rep.
15
48-54
2017
Mycobacterium tuberculosis (P9WN21), Mycobacterium tuberculosis H37Rv (P9WN21), Mycobacterium tuberculosis ATCC 25618 (P9WN21)
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