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ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ATP + D-mannose
ADP + 3-O-phospho-D-mannose
additional information
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ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
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-
?
ATP + 2-alpha-D-mannosyl-D-mannose
ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
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-
-
?
ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
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the substrate is an an 8-azidooctyl glycoside derivatives of the Escherichia coli serotype O9a O-chain repeating unit. WbdD shows dual kinase and methyltransferase activity
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-
?
ATP + 8-azidooctyl alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man
ADP + 8-azidooctyl 3-O-phospho-alpha-D-mannopyranosyl-(1->2)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranosyl-(1->3)-alpha-D-mannopyranoside
-
the substrate is an an 8-azidooctyl glycoside derivatives of the Escherichia coli serotype O9a O-chain repeating unit. WbdD shows dual kinase and methyltransferase activity
-
-
?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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overexpression of WbdD decreases O-polysaccharide chain length. O-Polysaccharide chain length is not reduced by overexpressing the heterologous plasmid encoded WbdD proteins. The WbdD proteins are therefore specific for a given serotype
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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overexpression of WbdD decreases O-polysaccharide chain length. O-Polysaccharide chain length is not reduced by overexpressing the heterologous plasmid encoded WbdD proteins. The WbdD proteins are therefore specific for a given serotype
-
-
?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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-
?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation
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-
?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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ATP + D-mannose
ADP + 3-O-phospho-D-mannose
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ATP + D-mannose
ADP + 3-O-phospho-D-mannose
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additional information
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enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities
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additional information
?
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enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the chain length of bacterial lipopolysaccharide O antigens is determined in the ATP-binding cassette (ABC) transporter-dependent pathway. Escherichia coli O8 polymannan is synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the lipopolysaccharide molecule. The polymannan O antigens has nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdDO8 enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdDO9a catalyzes both reactions
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-
?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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the phosphorylation of the O9a O-polysaccharide is a prerequisite for methylation. Terminal phosphorylation of the O9a repeating unit prevents polymer elongation by the mannosyltransferases and thus phosphorylation alone is sufficient for chain-length control of the O9a O-polysaccharide
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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?
ATP + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
ADP + 3-O-phospho-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
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?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
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construction of a chromosomal wbdDO9a::aacC1 mutation by allelic exchange. Membranes of the mutant are still able to synthesize O9a polymannan in vitro, although the chain length is increased relative to that made by the parent
malfunction
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membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
malfunction
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construction of a chromosomal wbdDO9a::aacC1 mutation by allelic exchange. Membranes of the mutant are still able to synthesize O9a polymannan in vitro, although the chain length is increased relative to that made by the parent
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malfunction
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membrane preparations from a wbdD mutant have severely diminished mannosyltransferase activity in vitro, and no significant amounts of the WbdA protein are targeted to the membrane fraction. Expression of a polypeptide comprising the WbdD C-terminal region is sufficient to restore both proper localization of WbdA and mannosyltransferase activity
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physiological function
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the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenol phosphate) in the inner (cytoplasmic) membrane. Chain extension is mediated by three mannosyltransferases, designated WbdCBA, and occurs by the addition of mannose residues to the non-reducing terminus of the glycan. The chain length of the O9a O-polysaccharide is controlled by the activity of the WbdD protein by addition of methylphosphate to the non-reducing terminus
physiological function
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the WbdD proteins control the chain length of the Escherichia coli O9a polymannan by modifying the nonreducing end of nascent undecaprenol diphosphate-linked polymer. Overexpression of WbdD decreases O-polysaccharide chain length. WbdD activity coordinates polymannan chain termination with export across the inner membrane
physiological function
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WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
physiological function
chain-terminator enzyme WbdD caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-antigen polysaccharide (O-PS) is exported and incorporated into LPS. Enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities. WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Direct interaction between the CBM and the terminal methyl group. CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export. Essential to this chain-length regulation strategy is a quality control mechanism on the ABC transporter protein complex, which ensures that only terminated (and chain-regulated) O-PS is exported for assembly on the cell surface. O-PS ABC transporters are composed of homodimers of the transmembrane domain protein (Wzm) and the nucleotide-binding domain protein (Wzt). Wzt possesses a C-terminal CBM, which is specific for its cognate O-PS. Binding of O-PS by the CBM is a prerequisite for transport, and removal or mutation of the CBM abrogates export. WbdD kinase activity is solely responsible for arresting O9a O-PS polymerization. Catalytic mechanism, overview
physiological function
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the WbdD proteins control the chain length of the Escherichia coli O9a polymannan by modifying the nonreducing end of nascent undecaprenol diphosphate-linked polymer. Overexpression of WbdD decreases O-polysaccharide chain length. WbdD activity coordinates polymannan chain termination with export across the inner membrane
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physiological function
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WbdD controls polymerization reaction in biosynthesis of the O-polysaccharide by coordinating the correct membrane association required for activity of one of the critical mannosyltransferases, WbdA. Identification of regions in the C terminus of WbdD that contribute to the interaction
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physiological function
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the glycan of the polymannose O-polysaccharide of Escherichia coli O9a is assembled on a 55-carbon lipid acceptor (undecaprenol phosphate) in the inner (cytoplasmic) membrane. Chain extension is mediated by three mannosyltransferases, designated WbdCBA, and occurs by the addition of mannose residues to the non-reducing terminus of the glycan. The chain length of the O9a O-polysaccharide is controlled by the activity of the WbdD protein by addition of methylphosphate to the non-reducing terminus
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physiological function
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chain-terminator enzyme WbdD caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-antigen polysaccharide (O-PS) is exported and incorporated into LPS. Enzyme WbdD is bifunctional and shows both kinase and methyltransferase activities. WbdD mutants reveal that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export. Direct interaction between the CBM and the terminal methyl group. CBM can bind the O-PS only with the native repeat unit, revealing that methylphosphate is essential but not sufficient for substrate recognition and export. Essential to this chain-length regulation strategy is a quality control mechanism on the ABC transporter protein complex, which ensures that only terminated (and chain-regulated) O-PS is exported for assembly on the cell surface. O-PS ABC transporters are composed of homodimers of the transmembrane domain protein (Wzm) and the nucleotide-binding domain protein (Wzt). Wzt possesses a C-terminal CBM, which is specific for its cognate O-PS. Binding of O-PS by the CBM is a prerequisite for transport, and removal or mutation of the CBM abrogates export. WbdD kinase activity is solely responsible for arresting O9a O-PS polymerization. Catalytic mechanism, overview
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additional information
structural requirements for glycan recognition by the CBM, overview
additional information
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structural requirements for glycan recognition by the CBM, overview
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D350A
88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
D351A
0.9% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.1% with substrate D-mannose
D351E
4.5% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.5% with substrate D-mannose
DELTA398-418
6.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 4.7% with substrate D-mannose
E274A
45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
H132A
complete loss of activity
H133A
complete loss of activity
N34D/Q35E/H197E
complete loss of activity
R203A
complete loss of activity
R270A
72.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 85.7% with substrate D-mannose
W355F
72.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.9% with substrate D-mannose
W355H
48.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 50.7% with substrate D-mannose
Y16F
complete loss of activity
Y230F
0.1% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 2.5% with substrate D-mannose
D350A
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88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
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E274A
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45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
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H132A
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complete loss of activity
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R203A
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complete loss of activity
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Y16F
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complete loss of activity
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additional information
uncoupling of WbdD kinase and methyltransferase activities, revealing that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
additional information
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uncoupling of WbdD kinase and methyltransferase activities, revealing that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
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Clarke, B.R.; Cuthbertson, L.; Whitfield, C.
Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter
J. Biol. Chem.
279
35709-35718
2004
Escherichia coli, Escherichia coli O9a
brenda
Clarke, B.R.; Greenfield, L.K.; Bouwman, C.; Whitfield, C.
Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway
J. Biol. Chem.
284
30662-30672
2009
Escherichia coli, Escherichia coli O9a
brenda
Clarke, B.R.; Richards, M.R.; Greenfield, L.K.; Hou, D.; Lowary, T.L.; Whitfield, C.
In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide; the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan
J. Biol. Chem.
286
41391-41401
2011
Escherichia coli, Escherichia coli O9a
brenda
Hagelueken, G.; Huang, H.; Harlos, K.; Clarke, B.R.; Whitfield, C.; Naismith, J.H.
Crystallization, dehydration and experimental phasing of WbdD, a bifunctional kinase and methyltransferase from Escherichia coli O9a
Acta Crystallogr. Sect. D
68
1371-1379
2012
Escherichia coli (J7I4B7), Escherichia coli O9a (J7I4B7)
brenda
Hagelueken, G.; Huang, H.; Clarke, B.R.; Lebl, T.; Whitfield, C.; Naismith, J.H.
Structure of WbdD: a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a
Mol. Microbiol.
86
730-742
2012
Escherichia coli (J7I4B7), Escherichia coli O9a (J7I4B7)
brenda
Mann, E.; Kelly, S.; Al-Abdul-Wahid, M.; Clarke, B.; Ovchinnikova, O.; Liu, B.; Whitfield, C.
Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a
J. Biol. Chem.
294
14978-14990
2019
Escherichia coli (J7I4B7)
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brenda