Literature summary for 2.7.1.167 extracted from

Lee, T.; Verhey, T.; Antiperovitch, P.; Atamanyuk, D.; Desroy, N.; Oliveira, C.; Denis, A.; Gerusz, V.; Drocourt, E.; Loutet, S.; Hamad, M.; Stanetty, C.; Andres, S.; Sugiman-Marangos, S.; Kosma, P.; Valvano, M.; Moreau, F.; Junop, M.
Structural-functional studies of Burkholderia cenocepacia D-glycero-beta-D-manno-heptose 7-phosphate kinase (HldA) and characterization of inhibitors with antibiotic adjuvant and antivirulence properties (2013), J. Med. Chem., 56, 1405-1417.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Burkholderia cepacia

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of enzyme-substrate and enzyme-product complexes and complexes with inhibitors [[2-({[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino}methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid and [[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid. Enzyme HldA is structurally similar to members of the PfkB carbohydrate kinase family and appears to catalyze heptose phosphorylation via an in-line mechanism mediated mainly by a conserved aspartate, Asp270. Both inhibitors adopt a folded conformation and occupy the nucleotide-binding sites	Burkholderia cepacia

Crystallization (Comment)

Organism

crystal structures of enzyme-substrate and enzyme-product complexes and complexes with inhibitors [[2-({[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino}methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid and [[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid. Enzyme HldA is structurally similar to members of the PfkB carbohydrate kinase family and appears to catalyze heptose phosphorylation via an in-line mechanism mediated mainly by a conserved aspartate, Asp270. Both inhibitors adopt a folded conformation and occupy the nucleotide-binding sites

Burkholderia cepacia

Inhibitors

Inhibitors	Comment	Organism	Structure
[[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid	binds to the nucleotide-binding sites without altering the overall structure of the enzyme or interfering with the binding of D-glycero-beta-D-manno-heptose-7-phosphate	Burkholderia cepacia
[[2-([[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid	binds to the nucleotide-binding sites without altering the overall structure of the enzyme or interfering with the binding of D-glycero-beta-D-manno-heptose-7-phosphate	Burkholderia cepacia

Organism

Organism	UniProt	Comment	Textmining
Burkholderia cepacia	B4EB35	-	-
Burkholderia cepacia J2315	B4EB35	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glycero-beta-D-manno-heptose 7-phosphate + ATP	-	Burkholderia cepacia	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP	-	?
D-glycero-beta-D-manno-heptose 7-phosphate + ATP	-	Burkholderia cepacia J2315	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP	-	?

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.00023	-	pH not specified in the publication, temperature not specified in the publication	Burkholderia cepacia	[[2-([[5-(2,6-dichlorophenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid
0.00081	-	pH not specified in the publication, temperature not specified in the publication	Burkholderia cepacia	[[2-([[5-(2,6-dimethoxyphenyl)-1,2,4-triazin-3-yl]amino]methyl)-1,3-benzothiazol-5-yl]oxy]acetic acid