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3.6.1.53: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase

This is an abbreviated version!
For detailed information about Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, go to the full flat file.

Word Map on EC 3.6.1.53

Reaction

ADP-D-ribose
+
H2O
=
AMP
 +
D-ribose 5-phosphate

Synonyms

ADP-ribose/CDP-alcohol diphosphatase, ADPRibase-I, ADPRibase-II, ADPRibase-Mn, Adprm, cADPR phosphohydrolase, Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase, Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase, More

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.53 Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase

Engineering

Engineering on EC 3.6.1.53 - Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H97A
severe reduction of activtiy
C253A
F210A
mutation lowers 40-70fold the catalytic efficiency for ADP-ribose, CDP-choline and 2',3'-cAMP hydrolysis, and 500fold for cyclic ADP-ribose
F37A
Phe37 is needed for ADP-ribose preference without catalytic effect
F37A/L196A
modest enhancement of the inhibitory effect over that of the F37A point mutation
F37A/L196F
modest enhancement of the inhibitory effect over that of the F37A point mutation
F37A/L196F/C253A
F37A/L196F/C253G
site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity
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
F37A/L196F/V252A/C253G
F37A/L196F/V252A/C253G/T279A
site-directed mutagenesis
F37Y
kinetic parameters similar to wild-type
H111A
marked decrease in efficiency with all substrates except 2',3'-cAMP
H111N
marked decrease in efficiency with all substrates except 2',3'-cAMP
L196A
modest 2-5fold decrease of catalytic efficiency with the substrates tested
N110A
reduction of catalytic efficiency is stronger for the hydrolysis of CDP-choline or 2',3'-cAMP than for the hydrolysis of ADP-ribose or cADPR. The decrease of kcat value is stronger for the hydrolysis of 2',3'-cAMP
Q27H
for ADP-ribose, modest negative effects of similar magnitude in catalysis and in substrate binding. For CDP-choline, the substitution affects only binding. For 2',3'-cAMP, the substitution affects catalysis, not binding
R43A
Arg43 is essential for catalysis, drastic efficiency loss of the mutant
additional information
design of mutations at or near residue 253 of human ADPRibase-Mn, in the vicinity of the adenine N1-linked (northern) ribose of cADPR, for altering the substrate specificity of the enzyme, overview