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Literature summary for 2.4.1.87 extracted from

  • Zhang, Y.; Deshpande, A.; Xie, Z.; Natesh, R.; Acharya, K.R.; Brew, K.
    Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase (2004), Glycobiology, 14, 1295-1302.
    View publication on PubMed
Search for more literature for 2.4.1.87

Cloned(Commentary)

Cloned (Comment) Organism
mutants W249G, W250Y, W250F, W315Y anf W356T, of catalytic domain are constructed and expressed in Escherichia coli BL21 Bos taurus

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion hanging drop method Bos taurus

Protein Variants

Protein Variants Comment Organism
W249G 1.95fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, turnover number of hydrolase reaction is identical to wild-type value, 2.1fold increase in Km-value for UDP-galactose in hydrolase reaction. Mutation does not affect the overall structure of the enzyme or its interactions with ligands Bos taurus
W250F 2.6fold increase in turnover number of galactosyltransferase reaction, 9.3fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 1.1fold decrease in Km-value for lactose, 1.4fold increase in turnover number of hydrolase reaction, 1.5fold increase in Km-value for UDP-galactose in hydrolase reaction Bos taurus
W250Y 1.2fold increase in turnover number of galactosyltransferase reaction, 5.2fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 2fold decrease in Km-value for lactose, 1.8fold increase in turnover number of hydrolase reaction, 2.3fold increase in Km-value for UDP-galactose in hydrolase reaction Bos taurus
W314Y 29fold decrease in turnover number of galactosyltransferase reaction, 1.67fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 2fold decrease in Km-value for lactose, 1.1fold increase in turnover number of hydrolase reaction, 1.4fold increase in Km-value for UDP-galactose in hydrolase reaction. Mutation does not affect the overall structure of the enzyme or its interactions with ligands Bos taurus
W356T 12.3fold decrease in turnover number of galactosyltransferase reaction, 2fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 6.3fold increase in Km-value for lactose, 14.5fold decrease in turnover number of hydrolase reaction, 2.5fold increase in Km-value for UDP-galactose in hydrolase reaction Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactose + lactose
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 Bos taurus UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
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 ?