2.7.1.181: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
This is an abbreviated version!
For detailed information about polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase, go to the full flat file.
Reaction
Synonyms
WbdD, WbdD kinase, WbdDO9a
ECTree
Advanced search results
Engineering
Engineering on EC 2.7.1.181 - polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
D350A
88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
D351A
0.9% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.1% with substrate D-mannose
D351E
4.5% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.5% with substrate D-mannose
DELTA398-418
6.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 4.7% with substrate D-mannose
E274A
45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
R270A
72.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 85.7% with substrate D-mannose
W355F
72.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.9% with substrate D-mannose
W355H
48.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 50.7% with substrate D-mannose
Y230F
0.1% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 2.5% with substrate D-mannose
D350A
-
88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose
-
E274A
-
45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose
-
additional information
uncoupling of WbdD kinase and methyltransferase activities, revealing that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
additional information
-
uncoupling of WbdD kinase and methyltransferase activities, revealing that although the kinase activity is solely responsible for chain-length regulation, both activities are essential for CBM recognition and export
-