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WbdA
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WbdA
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bifunctional alpha-(1->2)-, alpha-(1->3)-mannosyltransferase
WbdA
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trifunctional alpha-(1->2)-, alpha-(1->3)-, beta-(1->2)-mannosyltransferase
WbdA
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bifunctional alpha-(1->2)-, alpha-(1->3)-mannosyltransferase
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WbdA
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trifunctional alpha-(1->2)-, alpha-(1->3)-, beta-(1->2)-mannosyltransferase
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WbdA
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bifunctional alpha-(1->2)-, alpha-(1->3)-mannosyltransferase
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WbdA
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trifunctional alpha-(1->2)-, alpha-(1->3)-, beta-(1->2)-mannosyltransferase
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2 GDP-alpha-D-mannose + 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 = 2 GDP + [alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)]n+1-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-Man-(1->3)-alpha-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
(2)
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2 GDP-alpha-D-mannose + [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 = 2 GDP + 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
(1)
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GDP-alpha-D-mannose: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 2,3-alpha-mannosyltransferase (configuration-retaining)
The enzyme is involved in the biosynthesis of polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. The enzymes consists of two domains that are responsible for the 1->2 and 1->3 linkages, respectively.
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
additional information
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: the enzyme polymerizes a tetrasaccharide repeat unit containing two alpha-(1->3)- and two alpha-(1->2)-linked mannopyranose residues
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: -
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: the enzyme polymerizes a tetrasaccharide repeat unit containing two alpha-(1->3)- and two alpha-(1->2)-linked mannopyranose residues
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: -
Products: -
?
2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: the enzyme polymerizes a tetrasaccharide repeat unit containing two alpha-(1->3)- and two alpha-(1->2)-linked mannopyranose residues
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->2)-alpha-Manp-(1->2)-alpha-Manp-(1->3)-alpha-Manp
2 GDP + ?
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Substrates: -
Products: -
?
2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: the enzyme polymerizes trisaccharide repeat units containing single alpha-(1->3)-, alpha-(1->2)-, and beta-(1->2)-mannopyranoses
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: -
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: the enzyme polymerizes trisaccharide repeat units containing single alpha-(1->3)-, alpha-(1->2)-, and beta-(1->2)-mannopyranoses
Products: -
?
2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: -
Products: -
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2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: the enzyme polymerizes trisaccharide repeat units containing single alpha-(1->3)-, alpha-(1->2)-, and beta-(1->2)-mannopyranoses
Products: -
?
2 GDP-alpha-D-mannose + alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
2 GDP + ?
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Substrates: -
Products: -
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additional information
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Substrates: no activity with alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
Products: -
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additional information
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Substrates: the N-terminal domain of the enzyme possesses alpha-(1->2)-mannosyltransferase activity, and the C-terminal domain is an alpha-(1->3)-mannosyltransferase
Products: -
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additional information
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Substrates: no activity with alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
Products: -
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additional information
?
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Substrates: no activity with alpha-Manp-(1->3)-alpha-Manp-(1->3)-beta-GlcpNAc
Products: -
?
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Liston, S.D.; Clarke, B.R.; Greenfield, L.K.; Richards, M.R.; Lowary, T.L.; Whitfield, C.
Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen
J. Biol. Chem.
290
1075-1085
2015
Escherichia coli
brenda
Greenfield, L.; Richards, M.; Li, J.; Wakarchuk, W.; Lowary, T.; Whitfield, C.
Biosynthesis of the polymannose lipopolysaccharide O-antigens from Escherichia coli serotypes O8 and O9a requires a unique combination of single- and multiple-active site mannosyltransferases
J. Biol. Chem.
287
35078-35091
2012
Escherichia coli, Escherichia coli CWG634, Escherichia coli CWG636
brenda
Greenfield, L.; Richards, M.; Vinogradov, E.; Wakarchuk, W.; Lowary, T.; Whitfield, C.
Domain organization of the polymerizing mannosyltransferases involved in synthesis of the Escherichia coli O8 and O9a lipopolysaccharide O-antigens
J. Biol. Chem.
287
38135-38149
2012
Escherichia coli, Escherichia coli CWG634, Escherichia coli CWG636
brenda
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