EC Number   |
Protein Variants |
Reference  |
|---|
   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 |
mutation enhances GalNAc-transferase activity. Km for GlcNAc is incereased compared to the wild type |
489546 |
| 2.4.1.90 | Y289N |
mutation enhances GalNAc-transferase activity. Km for GlcNAc is increased compared to the wild type |
489546 |
| 2.4.1.90 | C134S |
complete loss of activity |
489552 |
| 2.4.1.90 | C342S |
33fold increase in the apparent Km-value for UDPgalactose |
489552 |
| 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 | D254E |
0.01% of the activity of the wild-type enzyme |
489556 |
| 2.4.1.90 | D254N |
0.01% of the activity of the wild-type enzyme |
489556 |
| 2.4.1.90 | D320A |
when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme |
489556 |
| 2.4.1.90 | D320E |
when partially activated by Mn2+ binding to the primary site, can be further activated by Co2+ or inhibited by Ca2+, an effect that is the opposite of what is observed with the wild-type enzyme |
489556 |
