EC Number   |
Protein Variants |
Reference |
|---|
   3.6.1.53 | C253A |
10fold increase of the catalytic efficiency for cyclic ADP-ribose |
735009 |
| 3.6.1.53 | C253A |
Cys253 is hindering for cADPR phosphohydrolase activity, specific tenfold gain of efficiency with cyclic ADP-ribose |
735009 |
| 3.6.1.53 | F210A |
mutation lowers 40-70fold the catalytic efficiency for ADP-ribose, CDP-choline and 2',3'-cAMP hydrolysis, and 500fold for cyclic ADP-ribose |
735009 |
| 3.6.1.53 | F37A |
Phe37 is needed for ADP-ribose preference without catalytic effect |
735009 |
| 3.6.1.53 | F37A/L196A |
modest enhancement of the inhibitory effect over that of the F37A point mutation |
735009 |
| 3.6.1.53 | F37A/L196F |
modest enhancement of the inhibitory effect over that of the F37A point mutation |
735009 |
| 3.6.1.53 | F37A/L196F/C253A |
cyclic ADP-ribose is the best substrate, with a 8fold increase in catalytic efficiency compared to wild-type |
735009 |
| 3.6.1.53 | F37A/L196F/C253A |
site-directed mutagenesis, specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase. Mutagenesis of human ADPRibase-Mn at Phe37, Leu196 and Cys253 alters its specificity, the best substrate of the mutant is cyclic ADP-ribose (cADPR), the Cys253 mutation is essential for cADPR preference. The proximity to the northern ribose of cADPR in docking models indicates Cys253 is a steric constraint for cADPR positioning |
758417 |
| 3.6.1.53 | F37A/L196F/C253G |
site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity |
758417 |
| 3.6.1.53 | F37A/L196F/D250A/C253G |
site-directed mutagenesis, the quadruple mutant shows a detrimental effect of the D250A substitution on the efficiency with all substrates (1.3-3.4fold decrease), and more markedly so for cADPR, such that the substrate efficiency ratios are less favourable than for the triple mutant F37A/ L196F/C253G |
758417 |
