2.4.1.44: lipopolysaccharide 3-alpha-galactosyltransferase

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For detailed information about lipopolysaccharide 3-alpha-galactosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.44

2.4.1.44

angiogenic

kinase-1

vasculogenesis

vegf-induced

fms-like

neuropilin-1

Reaction

3-alpha-D-galactosyl-[lipopolysaccharide glucose]

Synonyms

galactosyltransferase, lipopolysaccharide alpha, 3-, galactosyltransferase, uridine diphosphogalactose-lipopolysaccharide alpha,3-, UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase, UDP-galactose:polysaccharide galactosyltransferase, uridine diphosphate galactose:lipopolysaccharide alpha-3-galactosyltransferase, uridine diphosphogalactose-lipopolysaccharide alpha,3-galactosyltransferase, Wbby

ECTree

2 Transferases

2.4 Glycosyltransferases

2.4.1 Hexosyltransferases

2.4.1.44 lipopolysaccharide 3-alpha-galactosyltransferase

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Results	in table
4	Activating Compound
1628	AA Sequence
1	CAS Registry Number
1	Cloned(Commentary)
1	General Information
1	General Stability
1	Inhibitors
1	KM Value [mM]
2	Localization
3	Metals/Ions
8	Natural Substrates/ Products (Substrates)
5	Organism
4	Pathway
2	PDB ID
1	pH Optimum
1	pH Stability
2	Posttranslational Modification
2	Purification (Commentary)
1	Reaction
1	Reaction Type
5	Reference
4	Specific Activity [micromol/min/mg]
1	Storage Stability
15	Substrates and Products (Substrate)
7	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

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General Information on EC 2.4.1.44 - lipopolysaccharide 3-alpha-galactosyltransferase

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physiological function

Klebsiella pneumoniae

WbbY possesses two glycosyltransferase catalytic sites solely responsible for O1 antigen polymerization and forming a complex with the O2a glycosyltransferase WbbM. The C-terminal WbbY domain is a UDP-galactopyranoside-dependent GT-A galactosyltransferase adding beta-(1-3)-linked D-galalctopyranoside, whereas the WbbY N-terminus includes a GT-B enzyme adding alpha-(1-3)-linked D-galactofuranoside. These activities build the O1 antigen on a terminal galactopyranoside in the O2a domain

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