Literature summary for 2.4.1.90 extracted from

Ramakrishnan, B.; Qasba, P.K.
Structure-based design of beta 1,4-galactosyltransferase I (beta4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity (2002), J. Biol. Chem., 277, 20833-20839.

Search for more literature for 2.4.1.90

Activating Compound

Activating Compound	Comment	Organism	Structure
alpha-lactalbumin	stimulates transfer of galactose from UDPgalactose to N-acetylgalactosamine	Bos taurus

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Bos taurus

Protein Variants

Protein Variants	Comment	Organism
Y289I	mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type	Bos taurus
Y289L	mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type	Bos taurus
Y289N	mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type	Bos taurus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	required	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-GalNAc + GlcNAc	transfer of GalNAc is only 1% of galactose transfer in wild type enzyme. Mutant enzyme Y289L exhibits nearly 100% of the galactose transferase activity	Bos taurus	?	-	?
UDPgalactose + glucose	in presence of alpha-lactalbumin	Bos taurus	lactose + UDP	-	?
UDPgalactose + N-acetylglucosamine	-	Bos taurus	UDP + N-acetyllactosamine	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Bos taurus

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Release 2023.1 (January 2023)