EC Number |
Protein Variants |
Reference |
---|
2.4.2.30 | A425K |
site-directed mutagenesis, phenotypic analysis |
673573 |
2.4.2.30 | C19A |
ADP-ribosyltransferase activity is 118% of the wild-type activity |
-, 658013 |
2.4.2.30 | D187A |
catalytically inactive |
759710 |
2.4.2.30 | D424A |
site-directed mutagenesis, phenotypic analysis |
673573 |
2.4.2.30 | D424A/D427A |
site-directed mutagenesis, reduced interaction with 14-3-3, phenotypic analysis |
673573 |
2.4.2.30 | D424A/L426A/D427A/L428A |
site-directed mutagenesis, the mutant shows a highly reduced expression level, phenotypic analysis |
673573 |
2.4.2.30 | D427A |
site-directed mutagenesis, the mutant shows a reduced expression level, phenotypic analysis |
673573 |
2.4.2.30 | DELTA106-288 |
mutant enzyme has NADase activity, lack of transferase activity |
659225 |
2.4.2.30 | DELTA24288 |
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine |
659225 |
2.4.2.30 | DELTA24293 |
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine |
659225 |