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3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

This is an abbreviated version!
For detailed information about ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase, go to the full flat file.

Word Map on EC 3.2.2.6

Reaction

cyclic ADP-ribose
+
H2O
=
ADP-D-ribose

Synonyms

ADP-ribosyl cyclase, ADPR cyclase, bCD38, CD38, CD38/NAD+ glycohydrolase, NAD(P) nucleosidase, NAD(P)+ glycohydrolase, NAD(P)+-glycohydrolase, NAD(P)-glycohydrolase, NAD(P)ase, NAD+ glycohydrolase, NADase, nicotinamide adenine dinucleotide (phosphate) glycohydrolase, nicotinamide adenine dinucleotide (phosphate) nucleosidase, nucleosidase, nicotinamide adenine dinucleotide (phosphate), triphosphopyridine nucleotidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.6 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Engineering

Engineering on EC 3.2.2.6 - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D147A
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
E138A
site-directed mutagenesis, the mutation causes a modest increase in the rate of NAD+ transformation which is proportional to its concentration. At 4.0 M, the rate increase is about 1.2fold and the formation of beta-1'-O-methyl ADP-ribose amounts to about 80% of the total reaction products. The observed selectivity in favor of methanolysis is similar to that of wild-type enzyme. The ADP-ribosyl cyclase activity of E138A mutant is more affected by the competing nucleophile, i.e. formation of ADP-ribose and cADPR are reduced by 75% and 90% respectively at 4.0 M methanol, the mutant shows an increase in ADP cyclization and higly reduced overall activity compared to the wild-type enzyme
E138Q
site-directed mutagenesis, in the presence of methanol, mutant E138Q efficiently catalyzes the formation of beta-1'-O-methyl ADP-ribose. But in contrast with mutant E138A, and like the wild-type enzyme, solvolysis does not affect the overall turnover rate of NAD+ indicating that the formation of the E.ADP-ribosyl intermediate is still rate limiting
E218A
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
E218Q
K120A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R216A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S185A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W118A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate compared to the wild-type enzyme
W118A/W181A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate which is 16fold lower than the product of the effects of the two single mutations
W118F
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W118H
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W168A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W181A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate and a reduced sensitivity to nicotinamide inhibition compared to the wild-type enzyme
W181F
site-directed mutagenesis, the mutant shows a decrease in activity and an increase in ADP cyclization compared to the wild-type enzyme
E226D
E226Q
N100D
site-directed mutagenesis, N-glycoylation at the site is abolished
N164D
site-directed mutagenesis, N-glycoylation at the site is abolished
N209D
site-directed mutagenesis, N-glycoylation at the site is abolished
N219D
site-directed mutagenesis, N-glycoylation at the site is abolished
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