EC Number |
Protein Variants |
Reference |
---|
2.4.1.90 | more |
decreasing the expression of beta1,4GalT II using RNA interference inhibits p53-mediated HeLa cell apoptosis induced by adriamycin |
687455 |
2.4.1.90 | more |
mutations of Asp318 and Asp319 abolish enzyme activity |
489556 |
2.4.1.90 | more |
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+ |
489552 |
2.4.1.90 | more |
the enzyme transfected 7721 hepatocarcinoma cell line is more susceptible to cycloheximide-induced apoptosis than the wild-type cells, cells show increased enzyme activity and expression of Galbeta1,4GlcNAc groups on the cell surface |
659925 |
2.4.1.90 | W314A |
site-directed mutagenesis, mutant shows highly reduced activity, i.e. 0.6% of wild-type galactosyltransferase activity, substrate binding, and reduced binding to the effector alpha-lactalbumin as well as reduced susceptibility to cleavage by proteases Glu-C and Lys-C compared to the wild-type enzyme, overview |
659700 |
2.4.1.90 | Y268G/W294G |
inactive |
757209 |
2.4.1.90 | Y289I |
mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme |
658502 |
2.4.1.90 | Y289I |
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type |
489546 |
2.4.1.90 | Y289L |
mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme |
658502 |
2.4.1.90 | Y289L |
mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type |
489546 |