Literature summary for 3.1.3.82 extracted from

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 (2010), Biochemistry, 49, 1033-1041.

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Application

Application	Comment	Organism
medicine	the enzyme is a target for combatting Gram-negative bacterial infection	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
parental and mutant hexahistidine-tagged GmhB proteins are overexpressed	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor diffusion method at 20°C, native apoenzyme, SeMet apoenzyme, calcium bound enzyme and calcium and phosphate-bound enzyme	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C107A	kcat/Km for D-glycero-alpha,beta-D-manno-heptose 1,7-bisphosphate is 5fold lower than wild-type value	Escherichia coli
D11N	inactive	Escherichia coli
D13N	inactive	Escherichia coli
K111A	inactive	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.2	-	D-glycero-beta-D-manno-heptose 1,7-bisphosphate	pH 8.0, wild-type enzyme	Escherichia coli
0.7	-	D-glycero-beta-D-manno-heptose 1,7-bisphosphate	pH 8.0, mutant enzyme C107A	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the Zn2+ binding pocket does not appear to be involved directly in activity	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O	Escherichia coli	lipopolysaccharide is a major component of the outer membrane of Gram-negative bacteria and provides a permeability barrier to many commonly used antibiotics. ADP-heptose residues are an integral part of the LPS inner core, and mutants deficient in heptose biosynthesis demonstrate increased membrane permeability	D-glycero-beta-D-manno-heptose 1-phosphate + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P63228	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O	lipopolysaccharide is a major component of the outer membrane of Gram-negative bacteria and provides a permeability barrier to many commonly used antibiotics. ADP-heptose residues are an integral part of the LPS inner core, and mutants deficient in heptose biosynthesis demonstrate increased membrane permeability	Escherichia coli	D-glycero-beta-D-manno-heptose 1-phosphate + phosphate	-	?
D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O	it is suggested that GmhB functions through a phosphoaspartate intermediate	Escherichia coli	D-glycero-beta-D-manno-heptose 1-phosphate + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	crystallographic data	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
3	6	D-glycero-beta-D-manno-heptose 1,7-bisphosphate	pH 8.0, wild-type enzyme	Escherichia coli
17	-	D-glycero-beta-D-manno-heptose 1,7-bisphosphate	pH 8.0, mutant enzyme C107A	Escherichia coli

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Release 2023.1 (January 2023)