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Literature summary for 2.4.1.38 extracted from

  • Boeggeman, E.E.; Balajai, P.V.; Qasba, P.K.
    Functional domains of bovine beta-1,4-galactosyltransferase (1995), Glycoconjugate J., 12, 865-878.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Bos taurus

Protein Variants

Protein Variants Comment Organism
C134S complete loss of activity Bos taurus
C342S 33fold increase in the apparent Km-value for UDPgalactose Bos taurus
additional information N-terminal truncated forms of the enzyme between residues 1-129, do not show any significant difference in the apparent Km-values towards N-acetylglucosamine or linear oligosaccharide acceptors, e.g. for chitobiose and chitotriose, or for the nucleotide donor UDPgalactose. The binding behaviour of N-terminal and C-terminal fragments of the enzyme towards the N-acetylglucosamine-agarose and UDP-agarose columns differ, the former binds preferentially to the N-acetylglucosamine-columns, while the latter binds to UDP-agarose columns via Mn2+ Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDPgalactose + chitobiose
-
Bos taurus ?
-
?
UDPgalactose + chitotriose
-
Bos taurus ?
-
?
UDPgalactose + N-acetylglucosamine
-
Bos taurus UDP + N-acetyllactosamine
-
?