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Information on EC 3.1.3.82 - D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase and Organism(s) Escherichia coli and UniProt Accession P63228

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IUBMB Comments
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 .
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Escherichia coli
UNIPROT: P63228
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
D-heptose-1,7-bisphosphate phosphatase, more
PATHWAY SOURCE
PATHWAYS
-
-
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].
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 1-phosphate + phosphate
show the reaction diagram
poor substrate
-
-
?
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O
D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate
show the reaction diagram
kcat/Km for the beta-anomer is 100fold higher than for the alpha-anomer
-
-
?
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
-
-
-
?
additional information
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
contains Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glycero-beta-D-manno-heptose 1-phosphate
noncompetitive inhibitor
histidinol phosphate
noncompetitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
D-fructose 1,6-bisphosphate
pH 7.5, 25°C
0.032 - 0.3
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
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.039
D-fructose 1,6-bisphosphate
pH 7.5, 25°C
0.0017 - 4.6
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
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
D-fructose 1,6-bisphosphate
pH 7.5, 25°C
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
pH 7.5, 25°C
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of gmhB causes a partial defect in the synthesis of the lipopolysaccharide core, resulting in the formation of heptoseless and heptose-rich forms
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
gel filtration
24900
x * 24900, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 24900, SDS-PAGE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method at 20°C, native apoenzyme, SeMet apoenzyme, calcium bound enzyme and calcium and phosphate-bound enzyme
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C107A
C109A
kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 1400fold lower than wild-type value
C92A
kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 230fold lower than wild-type value
D13A
mutant is devoid of detectable activity toward the physiological substrate D-glycero-beta-D-manno-heptose 1,7-bisphosphate
K111A
inactive
K137A
kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 10fold lower than wild-type value
R110A
kcat/KM for D-glycero-beta-D-manno-heptose 1,7-bisphosphate is 230fold lower than wild-type value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed as His-tagged fusion protein
parental and mutant hexahistidine-tagged GmhB proteins are overexpressed
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme is a target for combatting Gram-negative bacterial infection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, P.L.; Sugiman-Marangos, S.; Zhang, K.; Valvano, M.A.; Wright, G.D.; Junop, M.S.
Structural and kinetic characterization of the LPS biosynthetic enzyme D-alpha,beta-D-heptose-1,7-bisphosphate phosphatase (GmhB) from Escherichia coli
Biochemistry
49
1033-1041
2010
Escherichia coli (P63228)
Manually annotated by BRENDA team
Wang, L.; Huang, H.; Nguyen, H.H.; Allen, K.N.; Mariano, P.S.; Dunaway-Mariano, D.
Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)
Biochemistry
49
1072-1081
2010
Bordetella bronchiseptica (Q7WG29), Escherichia coli (P63228), Mesorhizobium loti (Q98I56)
Manually annotated by BRENDA team
Nguyen, H.H.; Wang, L.; Huang, H.; Peisach, E.; Dunaway-Mariano, D.; Allen, K.N.
Structural determinants of substrate recognition in the HAD superfamily member D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB)
Biochemistry
49
1082-1092
2010
Escherichia coli (P63228), Bordetella bronchiseptica (Q7WG29)
Manually annotated by BRENDA team
Kneidinger, B.; Marolda, C.; Graninger, M.; Zamyatina, A.; McArthur, F.; Kosma, P.; Valvano, M.A.; Messner, P.
Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli
J. Bacteriol.
184
363-369
2002
Escherichia coli (P63228)
Manually annotated by BRENDA team