Information on EC 3.1.3.82 - D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.3.82
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RECOMMENDED NAME
GeneOntology No.
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ADP-L-glycero-beta-D-manno-heptose biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase
The enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. In vitro the catalytic efficiency with the beta-anomer is 100-200-fold higher than with the alpha-anomer [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
?
show the reaction diagram
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slow substrate
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?
D-fructose 1,6-bisphosphate + H2O
D-fructose 1-phosphate + phosphate
show the reaction diagram
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poor substrate
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?
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
D-glycero-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
D-sedoheptulose 1,7-bisphosphate + H2O
?
show the reaction diagram
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?
additional information
?
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no activity with: fructose 6-phosphate, fructose 1-phosphate, alpha-D-glucose 1,6-bisphosphate, beta-D-glucose 1,6-bisphosphate, alpha-D-mannose 1,6-bisphosphate, and beta-D-mannose 1,6-bisphosphate, histidinol
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-beta-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
D-glycero-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
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synthesis of ADP-D-beta-D-heptose in Escherichia coli requires three proteins, GmhA (sedoheptulose 7-phosphate isomerase), HldE (bifunctional D-beta-D-heptose 7-phosphate kinase/D-beta-D-heptose 1-phosphate adenylyltransferase), and GmhB (D,D-heptose 1,7-bisphosphate phosphatase)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glycero-beta-D-manno-heptose 1-phosphate
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noncompetitive inhibitor
histidinol
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histidinol phosphate
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noncompetitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.68 - 1.5
D-fructose 1,6-bisphosphate
0.032 - 0.58
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
0.005 - 0.7
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
0.61
D-sedoheptulose 1,7-bisphosphate
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pH 7.5, 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.039 - 0.55
D-fructose 1,6-bisphosphate
0.0017 - 5.9
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
0.34 - 35.7
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
0.51
D-sedoheptulose 1,7-bisphosphate
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pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
D-fructose 1,6-bisphosphate
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pH 7.5, 25C
0.006 - 69
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
3.5 - 7140
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
0.84
D-sedoheptulose 1,7-bisphosphate
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pH 7.5, 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.15
D-glycero-beta-D-manno-heptose 1-phosphate
1 - 6
histidinol
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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gel filtration
20000
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gel filtration
24900
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x * 24900, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 24900, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method, X-ray structures of the enzyme in a complex with Mg2+ and phosphate at 1.7 A resolution
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sitting-drop vapour-diffusion method at room temperature
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hanging-drop vapor diffusion method at 20C, native apoenzyme, SeMet apoenzyme, calcium bound enzyme and calcium and phosphate-bound enzyme
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the X-ray crystallographic structures of Escherichia coli GmhB in the apo form (1.6 A resolution), in a complex with Mg2+ and orthophosphate (1.8 A resolution), and in a complex with Mg2+ and D-glycero-beta-D-manno-heptose 1,7-bisphosphate are determined
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed as His-tagged fusion protein
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parental and mutant hexahistidine-tagged GmhB proteins are overexpressed
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C109A
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kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 1400fold lower than wild-type value
C92A
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kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 230fold lower than wild-type value
D11N
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inactive
D13A
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mutant is devoid of detectable activity toward the physiological substrate D-glycero-beta-D-manno-heptose 1,7-bisphosphate
D13N
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inactive
K111A
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inactive
K137A
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kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 10fold lower than wild-type value
R110A
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kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 230fold lower than wild-type value
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the enzyme is a target for combatting Gram-negative bacterial infection