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ADP-alpha-D-mannose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
?
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. ADP-alpha-D-mannose is a poor substrate
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?
ADP-alpha-D-mannose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + ?
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i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. In cell extracts, ADP-mannose can serve as an alternative donor, but is mannosylated at less than 1% the rate of alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
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-
?
ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme transfers L-glycero-D-manno-heptose to a 3-deoxy-alpha-D-oct-2-ulopyranosonic acid of the growing core region of lipopolysaccharide. The catalytic efficiency of the enzyme with the fully deacylated analogue of Escherichia coli HepI Lipid A is 12fold greater than with the fully acylated substrate
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme transfers L-glycero-D-manno-heptose to a 3-deoxy-alpha-D-oct-2-ulopyranosonic acid of the growing core region of lipopolysaccharide. The catalytic efficiency of the enzyme with the fully deacylated alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A is 12fold greater than with the fully acylated substrate
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ADP-L-glycero-beta-D-manno-heptose + a 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid of the growing core region of lipopolysaccharide
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ADP-L-glycero-beta-D-manno-heptose + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP + alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP-L-glycero-beta-D-manno-heptose + lipopolysaccahride from Salmonella minnesota R595
ADP + ?
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ADP-L-glycero-beta-D-manno-heptose + O-deacylated Kdo2-lipidA
?
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additional information
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. Characterization of ADP-L-glycero-beta-D-manno-heptose as the physiological substrate
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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i.e. alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA. It is possible to assay the enzyme in crude cell extracts using ADP-mannose in place of ADP-L-glycero-beta-D-manno-heptose. No activity without detergent
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme is essential for the transfer of the first heptosyl moiety in the core oligosaccharide of lipopolysaccharide
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme is involved in the synthesis of the inner core region of lipopolysaccharide. It catalyzes the addition of the first L-glycero-D-manno-heptose (heptose) molecule to one 3-deoxy-D-manno-oct-2-ulosonic acid residue of the Kdo2-lipid A molecule. Heptose is an essential component of the lipopolysaccharide core domain. Its absence results in a truncated lipopolysaccharide associated with the deeprough phenotype causing a greater susceptibility to antibiotic and an attenuated virulence for pathogenic Gram-negative bacteria
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ADP-L-glycero-beta-D-manno-heptose + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP + alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
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ADP-L-glycero-beta-D-manno-heptose + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP + alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
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ADP-L-glycero-beta-D-manno-heptose + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP + alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
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ADP-L-glycero-beta-D-manno-heptose + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
ADP + alpha-Hep-(1->5)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
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additional information
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characterization of ADP-L-glycero-beta-D-manno-heptose as the physiological substrate
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additional information
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characterization of ADP-L-glycero-beta-D-manno-heptose as the physiological substrate
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additional information
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the enzyme is able to catalyze heptose transfer to underacylated and fully deacylated Kdo2-lipid A analogs. This activity does not require addition of detergent. Thus, the enzyme appears to only recognize the Kdo sugar region of these acceptor molecules
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additional information
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the enzyme is able to catalyze heptose transfer to underacylated and fully deacylated Kdo2-lipid A analogs. This activity does not require addition of detergent. Thus, the enzyme appears to only recognize the Kdo sugar region of these acceptor molecules
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additional information
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the purified enzyme displays no activity with ADP-glucose, GDP-mannose, UDP-glucose, or UDP-galactose
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP-L-glycero-beta-D-manno-heptose + a 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid of the growing core region of lipopolysaccharide
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additional information
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme is essential for the transfer of the first heptosyl moiety in the core oligosaccharide of lipopolysaccharide
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ADP-L-glycero-beta-D-manno-heptose + (3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
ADP + alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
the enzyme is involved in the synthesis of the inner core region of lipopolysaccharide. It catalyzes the addition of the first L-glycero-D-manno-heptose (heptose) molecule to one 3-deoxy-D-manno-oct-2-ulosonic acid residue of the Kdo2-lipid A molecule. Heptose is an essential component of the lipopolysaccharide core domain. Its absence results in a truncated lipopolysaccharide associated with the deeprough phenotype causing a greater susceptibility to antibiotic and an attenuated virulence for pathogenic Gram-negative bacteria
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additional information
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characterization of ADP-L-glycero-beta-D-manno-heptose as the physiological substrate
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additional information
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characterization of ADP-L-glycero-beta-D-manno-heptose as the physiological substrate
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-dec-2-ene-beta-D-galactopyranoside
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(2E)-dec-2-ene-beta-D-glucopyranoside
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(2E)-hept-2-ene-beta-D-galactopyranoside
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(2E)-hept-2-ene-beta-D-glucopyranoside
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(2E)-hex-2-ene-beta-D-galactopyranoside
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(2E)-hex-2-ene-beta-D-glucopyranoside
-
-
(2E)-oct-2-ene-alpha-D-galactopyranoside
-
-
(2E)-oct-2-ene-alpha-D-glucopyranoside
-
-
(2E)-oct-2-ene-beta-D-galactopyranoside
-
-
(2E)-oct-2-ene-beta-D-glucopyranoside
-
-
2-aryl-5-methyl-4-(5-aryl-furan-2-yl-methylene)-2,4-dihydro-pyrazol-3-one
micromolar inhibitors are identified by virtual screening, promising lead series for further optimization as antivirulence drug
3-[(4Z)-4-([5-[3-(methoxycarbonyl)phenyl]furan-2-yl]methylidene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
3-[(4Z)-4-[[5-(3-acetylphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
3-[(4Z)-4-[[5-(3-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
3-[(4Z)-4-[[5-(4-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
4-(5-[(Z)-[1-(3-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-methylbenzoic acid
-
4-[(4Z)-3-methyl-5-oxo-4-[(5-phenylfuran-2-yl)methylidene]-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
4-[(4Z)-4-[[5-(3-carbamoylphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
4-[(4Z)-4-[[5-(4-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
5-(5-[(Z)-[1-(3-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-chlorobenzoic acid
-
5-(5-[(Z)-[1-(4-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-chlorobenzoic acid
-
adenosine 5'-diphospho-2-deoxy-2-fluoro-L-glycero-beta-D-gluco-heptopyranoside
competitive inhibitor
allyl-beta-D-galactopyranoside
allyl-beta-D-glucopyranoside
decene-beta-D-galactopyranoside
-
5% inhibition
-
decene-beta-D-glucopyranoside
-
23.4% inhibition
-
glycofullerene
the average affinity of a single glycoside of the fullerenes towards WaaC is significantly enhanced when displayed as a multimer
-
heptene-beta-D-galactopyranoside
-
7.8% inhibition
-
heptene-beta-D-glucopyranoside
-
11.9% inhibition
-
hexene-beta-D-galactopyranoside
-
22.6% inhibition
-
hexene-beta-D-glucopyranoside
-
29.7% inhibition
-
kanamycin B
competitive inhibition
methyl-alpha-D-galactopyranoside
methyl-alpha-D-glucopyranoside
methyl-beta-D-galactopyranoside
methyl-beta-D-glucopyranoside
n-octyl-beta-D-glucopyranoside
neomycin
competitive inhibition
octene-alpha-D-galactopyranoside
-
8.8% inhibition
-
octene-alpha-D-glucopyranoside
-
16.7% inhibition
-
octene-beta-D-galactopyranoside
-
6.3% inhibition
-
octene-beta-D-glucopyranoside
-
4.2% inhibition
-
streptomycin
non-competitive inhibition
tobramycin
mixed competitive inhibition
Triton X-100
-
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
additional information
-
alkylated monosaccharides inhibit heptosyltransferase I. Compounds are uncompetitive with sugar acceptor substrate. Compounds have mixed inhibition with sugar donor substrate. Docking revealed putative allosteric inhibition pocket
-
allyl-beta-D-galactopyranoside
-
-
allyl-beta-D-galactopyranoside
-
10% inhibition
allyl-beta-D-glucopyranoside
-
-
allyl-beta-D-glucopyranoside
-
19.6% inhibition
D-galactose
-
-
D-galactose
-
28.5% inhibition
D-glucose
-
-
D-glucose
-
36% inhibition
methyl-alpha-D-galactopyranoside
-
-
methyl-alpha-D-galactopyranoside
-
8.8% inhibition
methyl-alpha-D-glucopyranoside
-
-
methyl-alpha-D-glucopyranoside
-
27.8% inhibition
methyl-beta-D-galactopyranoside
-
-
methyl-beta-D-galactopyranoside
-
7% inhibition
methyl-beta-D-glucopyranoside
-
-
methyl-beta-D-glucopyranoside
-
19.5% inhibition
n-octyl-beta-D-glucopyranoside
-
-
n-octyl-beta-D-glucopyranoside
-
8.3% inhibition
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00028 - 0.0005
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
0.009 - 0.029
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
0.0004 - 0.0009
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
0.0045
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
-
pH 7.5, 30°C
0.016 - 0.046
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
1.5
ADP-alpha-D-mannose
-
pH 7.5, 30°C
0.0025 - 0.015
ADP-L-glycero-beta-D-manno-heptose
0.0014 - 0.056
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
0.00028
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
0.0005
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
0.009
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
0.029
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
0.0004
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
0.0009
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
0.016
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
0.046
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
0.0025
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R61A
0.0029
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, wild-type enzyme
0.006
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R60A
0.008
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R64A
0.01
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R63A
0.015
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R120A
0.0014
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R60A
-
0.0025
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R61A
-
0.0029
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, wild-type enzyme
-
0.0029
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R61A
-
0.006
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R189A
-
0.006
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A
-
0.008
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A
-
0.01
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R63A
-
0.011
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R63A
-
0.014
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K192A
-
0.015
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A
-
0.016
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K98A
-
0.02
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A
-
0.034
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/K64A
-
0.037
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61/R60A
-
0.04
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A
-
0.056
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A/R63A/R64A
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.76 - 1.05
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
4.7 - 6.6
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
1.06 - 1.47
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
1.06 - 8
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
0.198 - 0.41
ADP-L-glycero-beta-D-manno-heptose
0.116 - 0.47
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
0.76
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
1.05
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
4.7
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
6.6
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
1.06
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
1.47
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
1.06
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
8
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
0.198
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R60A
0.32
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R120A
0.33
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R64A
0.36
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, wild-type enzyme
0.36
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R61A
0.41
ADP-L-glycero-beta-D-manno-heptose
pH 7.5, 37°C, mutant enzyme R63A
0.116
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R189A
-
0.14
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K192A
-
0.198
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A
-
0.2
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A
-
0.21
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A/R60A
-
0.21
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K98A
-
0.25
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A
-
0.26
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R61A
-
0.28
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A/R63A/R64A
-
0.281
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R60A
-
0.32
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A
-
0.33
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A
-
0.36
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, wild-type enzyme
-
0.36
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R61A
-
0.37
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R63A
-
0.41
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R63A
-
0.47
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/K64A
-
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2100 - 2700
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
220 - 520
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
1100 - 3700
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
170 - 340
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
5 - 200
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
2100
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
2700
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-amino-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-amino-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
220
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
520
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
1100
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
3700
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
170
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, in absence of detergent
340
(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-(tetradecanoyloxy)tetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH and temperature not specified in the publication, with Triton X-100
5
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A/R63A/R64A
-
6
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A/R60A
-
7
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A
-
10
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A
-
11
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K192A
-
13.1
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K98A
-
14
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/K64A
-
19
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R189A
-
21
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A
-
30
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R63A
-
33
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R60A
-
41
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme K64A
-
41
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R63A
-
90
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R61A
-
124
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, wild-type enzyme
-
140
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R61A
-
200
alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
pH 7.5, 37°C, mutant enzyme R120A/R60A
-
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0.52
(2E)-dec-2-ene-beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.57
(2E)-hex-2-ene-beta-D-galactopyranoside
-
pH and temperature not specified in the publication
0.34
(2E)-hex-2-ene-beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.049
3-[(4Z)-4-([5-[3-(methoxycarbonyl)phenyl]furan-2-yl]methylidene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.015
3-[(4Z)-4-[[5-(3-acetylphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.002
3-[(4Z)-4-[[5-(3-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.003
3-[(4Z)-4-[[5-(4-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.031
4-(5-[(Z)-[1-(3-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-methylbenzoic acid
pH and temperature not specified in the publication
0.055
4-[(4Z)-3-methyl-5-oxo-4-[(5-phenylfuran-2-yl)methylidene]-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.018
4-[(4Z)-4-[[5-(3-carbamoylphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.051
4-[(4Z)-4-[[5-(4-carboxyphenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
pH and temperature not specified in the publication
0.001
5-(5-[(Z)-[1-(3-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-chlorobenzoic acid
pH and temperature not specified in the publication
0.0031
5-(5-[(Z)-[1-(4-carboxyphenyl)-3-methyl-5-oxo-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)-2-chlorobenzoic acid
pH and temperature not specified in the publication
0.65
allyl-beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.004258
amikacin
pH 7.5, 37°C, wild-type enzyme
0.5
D-galactose
-
pH and temperature not specified in the publication
0.28
D-glucose
-
pH and temperature not specified in the publication
0.57
hexene-beta-D-galactopyranoside
-
pH and temperature not specified in the publication
-
0.34
hexene-beta-D-glucopyranoside
-
pH and temperature not specified in the publication
-
0.00099
kanamycin B
pH 7.5, 37°C, wild-type enzyme
0.37
methyl-alpha-D-glucopyranoside
-
pH and temperature not specified in the publication
0.68
methyl-beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.001643
neomycin
pH 7.5, 37°C, wild-type enzyme
0.000595 - 0.00789
streptomycin
0.000422 - 0.0034
tobramycin
0.000595
streptomycin
pH 7.5, 37°C, wild-type enzyme
0.0058
streptomycin
pH 7.5, 37°C, mutant enzyme R64A
0.006254
streptomycin
pH 7.5, 37°C, mutant enzyme R60A
0.0067
streptomycin
pH 7.5, 37°C, mutant enzyme R63A
0.00789
streptomycin
pH 7.5, 37°C, mutant enzyme R61A
0.000422
tobramycin
pH 7.5, 37°C, mutant enzyme R120A
0.001125
tobramycin
pH 7.5, 37°C, wild-type enzyme
0.0034
tobramycin
pH 7.5, 37°C, mutant enzyme R60A
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drug target
knockouts of WaaC have decreased virulence and increased susceptibility to antibiotics, making WaaC a potential drug target
drug target
disruption of the enzyme (HepI) increases susceptibility of bacteria to hydrophobic antibiotics, making HepI a potential target for drug development
drug target
fighting bacterial infections by inhibition of the enzyme (HepI) by aminoglycosides
drug target
-
disruption of the enzyme (HepI) increases susceptibility of bacteria to hydrophobic antibiotics, making HepI a potential target for drug development
-
drug target
-
fighting bacterial infections by inhibition of the enzyme (HepI) by aminoglycosides
-
evolution
redundancy of residues mediating conformational transitions in HepI illustrates the evolutionary importance of these structural rearrangements for catalysis
evolution
-
redundancy of residues mediating conformational transitions in HepI illustrates the evolutionary importance of these structural rearrangements for catalysis
-
malfunction
-
lipopolysaccharide isolated from mutants defective in rfaC lack heptose and all other sugars distal to heptose
malfunction
knockouts of WaaC have decreased virulence and increased susceptibility to antibiotics
malfunction
disruption of the enzyme (HepI) increases susceptibility of bacteria to hydrophobic antibiotics
malfunction
mutation in the waaC gene results in the expression of a severely truncated lipooligosaccharide compared to wild-type strain
malfunction
-
mutation in the waaC gene results in the expression of a severely truncated lipooligosaccharide compared to wild-type strain
-
malfunction
-
disruption of the enzyme (HepI) increases susceptibility of bacteria to hydrophobic antibiotics
-
metabolism
-
the enzyme catalyzes the addition of the first L-glycero-D-manno-heptose to the inner 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) residue of the Kdo2-Lipid A molecule in lipopolysaccharide which plays a role in adhesion to surfaces and formation of biofilms
metabolism
the enzyme transfers a heptose residue onto the endotoxin inner core structure (ReLPS) of the outer membrane
physiological function
the enzyme catalyzes the incorporation of the first L-heptose into lipopolysaccharide
physiological function
the enzyme is essential for the transfer of the first heptosyl moiety in the core oligosaccharide of lipopolysaccharide
physiological function
the enzyme is involved in the synthesis of the inner core region of lipopolysaccharide. It catalyzes the addition of the first L-glycero-D-manno-heptose (heptose) molecule to one 3-deoxy-D-manno-oct-2-ulosonic acid residue of the Kdo2-lipid A molecule. Heptose is an essential component of the lipopolysaccharide core domain. Its absence results in a truncated lipopolysaccharide associated with the deeprough phenotype causing a greater susceptibility to antibiotic and an attenuated virulence for pathogenic Gram-negative bacteria
physiological function
critical role in the biosynthesis of lipopolysaccharides on bacterial cell surfaces
physiological function
-
essential enzyme for the biosynthesis of the lipopolysaccharide
physiological function
essential enzyme for the biosynthesis of the lipopolysaccharide
physiological function
heptosyltransferase I catalyzes the transfer of the first L-glycero-D-manno-heptose residue to 3-deoxy-D-manno-octulosonic residue (Kdo)-lipid A
physiological function
-
heptosyltransferase I catalyzes the transfer of the first L-glycero-D-manno-heptose residue to 3-deoxy-D-manno-octulosonic residue (Kdo)-lipid A
-
physiological function
-
essential enzyme for the biosynthesis of the lipopolysaccharide
-
physiological function
-
essential enzyme for the biosynthesis of the lipopolysaccharide
-
physiological function
-
critical role in the biosynthesis of lipopolysaccharides on bacterial cell surfaces
-
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K192A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
K64A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
K64A/R63A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
K64A/R63A/R61A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]. Complete loss in blue shift, as well as an increase in the Apo lambda(max)
K64A/R63A/R61A/R60A
mutant enzyme with an 18-fold increase in KM, most likely because the mutations lead to structural changes in the alpha 3-N-5 loop thus impairing formation of the Michaelis complex. Complete loss in blue shift, as well as an increase in the Apo lambda(max)
K98A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherschia coli Kdo2-lipid A]
R120A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
R120A/K64A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]. Mutant enzyme displays an increase in protein unfolding
R120A/R60A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]. Mutant enzyme displays an increase in protein unfolding
R120A/R61A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]. Mutant enzyme displays an increase in protein unfolding
R120A/R63A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]. Mutant enzyme displays an increase in protein unfolding
R189A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
R60A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
R60A/R63A/R64A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
R61A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
R63A
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
K192A
-
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
K64A
-
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
R60A
-
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
R61A
-
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
R63A
-
decrease in kcat/Km for alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]
-
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Czyzyk, D.J.; Liu, C.; Taylor, E.A.
Lipopolysaccharide biosynthesis without the lipids: recognition promiscuity of Escherichia coli heptosyltransferase I
Biochemistry
50
10570-10572
2011
Escherichia coli (P24173), Escherichia coli
brenda
Moreau, F.; Desroy, N.; Genevard, J.M.; Vongsouthi, V.; Gerusz, V.; Le Fralliec, G.; Oliveira, C.; Floquet, S.; Denis, A.; Escaich, S.; Wolf, K.; Busemann, M.; Aschenbrenner, A.
Discovery of new Gram-negative antivirulence drugs: structure and properties of novel E. coli WaaC inhibitors
Bioorg. Med. Chem. Lett.
18
4022-4026
2008
Escherichia coli (P24173)
brenda
Durka, M.; Buffet, K.; Lehl, J.; Holler, M.; Nierengarten, J.F.; Vincent, S.P.
The inhibition of liposaccharide heptosyltransferase WaaC with multivalent glycosylated fullerenes: a new mode of glycosyltransferase inhibition
Chemistry
18
641-651
2011
Escherichia coli (P24173)
brenda
Gronow, S.; Brabetz, W.; Brade, H.
Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli
Eur. J. Biochem.
267
6602-6611
2000
Escherichia coli (P24173), Escherichia coli
brenda
Kadrmas, J.L.; Raetz, C.R.
Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase I
J. Biol. Chem.
273
2799-2807
1998
Escherichia coli
brenda
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Characterization of the physiological substrate for lipopolysaccharide heptosyltransferases I and II
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