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3.6.1.17: bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

This is an abbreviated version!
For detailed information about bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), go to the full flat file.

Word Map on EC 3.6.1.17

Reaction

P1,P4-bis(5'-guanosyl) tetraphosphate
+
H2O
=
GTP
 +
GMP

Synonyms

(asymmetrical) diadenosine 5',5''‚-P1,P4-tetraphosphate hydrolase, (asymmetrical) dinucleoside tetraphosphatase, Ap4A hydrolase, Ap4A-hydrolase, AP4AASE, Apf, asym-di-GDPase, asymmetric Ap4A hydrolase, asymmetric diadenosine tetraphosphate hydrolase, asymmetrical Ap4A hydrolase, asymmetrical bis-(5'-nucleosidyl)-tetraphosphatase, asymmetrical diadenosine tetraphosphate hydrolase, AtNUDX25 protein, ATP-producing Ap4A hydrolase, bis(5'-adenosyl)-tetraphosphatase, bis(5'-guanosyl)-tetraphosphatase, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), bis(5-guanosyl)tetraphosphatase, CT771, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase, diadenosine 5',5'-P1P4 tetraphosphate hydrolase, diadenosine 5,5-P1,P4-tetraphosphate hydrolase, diadenosine P1,P4-tetraphosphatase, Diadenosine tetraphosphatase, diadenosine tetraphosphate pyrophosphohydrolase, diguanosine tetraphosphatase, diguanosinetetraphosphatase (asymmetrical), diguanosinetetraphosphate guanosylhydrolase, dinucleoside tetraphosphatase, dinucleosidetetraphosphatase (asymmetrical), DIPP1, ENPP4, More, MXAN_1509, NDX-4, nudH, Nudix hydrolase, NUDT2, PFE1035c, PrpA

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.17 bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

Engineering

Engineering on EC 3.6.1.17 - bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E103Q
-
turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
E52Q
-
turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value
E56Q
-
turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value
H31A
-
turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme
H31V
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme
H38G
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
H38K
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value
K36M
-
turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme
K79M
-
turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme
K81M
-
turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme
K83M
-
turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme
Y121A
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme
Y27A
-
turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme
Y27D
-
turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme
Y76A
-
turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme
Y76A/Y121A
-
turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme
E58A
crystallization data
T70A
active site mutant, has no effect on platelet aggregation and secretion
E122Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 20% of the wild-type value, turnover-number is 50% of the wild-type value. 2.3fold reduction in sensitivity to fluoride
E125Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser. KM-value is 0.7% of the wild-type value, turnover-number is 56% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 83fold reduction in sensitivity to fluoride
E55Q
-
fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser. KM-value is 4.8% of the wild-type value, turnover-number is 0.01% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. More than 330fold reduction in sensitivity to fluoride
E58D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 38.4% of the wild-type value, turnover-number is 9% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 16.7fold reduction in sensitivity to fluoride
E58Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 80% of the wild-type value, turnover-number is 43.9% of the wild-type value. 6.7fold reduction in sensitivity to fluoride
E59D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 4fold higher than the wild-type value, turnover-number is 0.02% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. 2fold reduction in sensitivity to fluoride
E59Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 2.4fold higher than the wild-type value, turnover-number is 0.00076% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected
R54Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 330fold reduction in sensitivity to fluoride
P133A
5fold increase in Km value
P133F
3fold decrease in kcat value