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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) Bordetella bronchiseptica and UniProt Accession Q7WG29

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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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Bordetella bronchiseptica
UNIPROT: Q7WG29
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The taxonomic range for the selected organisms is: Bordetella bronchiseptica
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
?
show the reaction diagram
slow 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 150fold 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
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
enzyme contains Mg2+
Zn2+
GmhB possess a classical CxH-(x)nCxC motif that coordinates the Zn2+ with square planar geometry
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.68
D-fructose 1,6-bisphosphate
-
0.28
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
0.0069
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55
D-fructose 1,6-bisphosphate
-
5.9
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
22
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
3188
D-glycero-beta-D-manno-heptose 1,7-bisphosphate
pH 7.5, 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 20000, crystallographic data
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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