Substrate specificity of ADPRibase-Mn enzymes.
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KM and kcat/KM values for zebrafish wild-type and mutant enzyme are shown as means±S.D. (n = 3–6), and kcat values are derived from them.
aNeither the zebrafish wild type nor the rat enzyme display significant activity towards ADP-glucose, UDP-glucose, CDP-glucose, CDP, CMP, AMP or 3′,5′-cAMP.
bData taken from [11], [12].
cThe kinetic parameters of 2′,3′-cAMP hydrolysis correspond to the total activity, including the 3′-AMP-forming hydrolysis of the P-O2′ and the 2′-AMP-forming hydrolysis of the P-O3′ linkage. However, given the strong predominance of the P-O2′ linkage hydrolysis, the parameters may be reasonable approximations to this reaction kinetics.
dEstimated from the potency of (competitive) inhibition of ADP-ribose hydrolysis by cADPR.
end, not determined.
创建时间：
2012-07-27
