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3.6.1.9: nucleotide diphosphatase

This is an abbreviated version!
For detailed information about nucleotide diphosphatase, go to the full flat file.

Word Map on EC 3.6.1.9

Reaction

a nucleoside triphosphate
+
H2O
=
A nucleotide
 +
diphosphate

Synonyms

ADPglucose pyrophosphatase/phosphodiesterase, AGPPase, AGPPase1, AGPPase2, alkaline sphingomyelinase nucleotide pyrophosphatase phosphodiesterase 7, Apyrase, ASMTL-Maf, BSU28050, CBS-PPase, CBS-pyrophosphatase, CD203c, CD39, diphosphopyridine nucleotide pyrophosphatase, dITP pyrophosphatase, dITPase, E-NPP, E-NPP1, E-NPP3, E-NTPDase, E-type ATPDase, EC 3.6.1.19, ecto-ATP-diphosphohydrolase, ecto-ATPDase, ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleoside triphosphate diphosphohydrolase 2, ecto-nucleotide phosphodiesterase/pyrophosphatase 6 eNPP6, ecto-nucleotide pyrophosphatase, ecto-nucleotide pyrophosphatase/phosphodiesterase, ecto-nucleotide pyrophosphatase/phosphodiesterase I-3, ecto-nucleotide pyrophosphatase/phosphodiesterase1, ecto-nucleotide pyrophosphatase/phosphodiesterase3, ecto-nucleotide pyrophosphatase/phosphodiesterases, ectonucleotide pyrophosphatase/phosphodiesterase, ectonucleotide pyrophosphatase/phosphodiesterase 1, ectonucleotide pyrophosphatase/phosphodiesterase family member 3, ENPP1, ENPP3, ENTPD1, Entpd6, family II pyrophosphatase, h-NPP-1, h-NPP-3, h-NPP1, h-NPP3, HAM1, inosine triphosphatase, inosine triphosphate pyrophosphatase, inosine triphosphate pyrophosphohydrolase, ITPA, ITPase, Maf protein, Maf-like protein YhdE, MazG, MazG protein, MazG-related protein, More, MutT, NPP, NPP 1, NPP 2, NPP 3, NPP-5, NPP1, NPP2, NPP3, NPP6, NPP7, NPPase, NPPr, NTPDase, nucleoside triphosphate diphosphatase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate pyrophosphatase, nucleoside triphosphate pyrophosphohydrolase, nucleoside-triphosphate pyrophosphatase, nucleotide pyrophosphastases/phosphodiesterases1, nucleotide pyrophosphastases/phosphodiesterases3, nucleotide pyrophosphatase, nucleotide pyrophosphatase-1, nucleotide pyrophosphatase-3, nucleotide pyrophosphatase-5, nucleotide pyrophosphatase/phosphodiesterase, nucleotide pyrophosphatase/phosphodiesterase 1, nucleotide pyrophosphatase/phosphodiesterase NPP1, nucleotide pyrophosphatase/phosphodiesterase-1, nucleotide pyrophosphatase/phosphodiesterase-I, nucleotide pyrophosphatase/phosphodiesterases, nucleotide pyrophosphohydrolase, nucleotide-sugar pyrophosphatase, nucleotide-sugar pyrophosphatase/phosphodiesterase, ONPP, PC-1, plasma cell membrane glycoprotein-1, PPase, pyrophosphatase, nucleoside triphosphate, RdgB, RS21-C6, SAGPPase1, SAGPPase2, Tm-MazG, TM0159, TM0913, YhdE, YJR069C, YOR111W, ZmNPP1, ZmNPP2, ZmNPP3

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.9 nucleotide diphosphatase

Engineering

Engineering on EC 3.6.1.9 - nucleotide diphosphatase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E322A
-
site-directed mutagenesis
E322Y
-
site-directed mutagenesis
R166S
-
site-directed mutagenesis
R166S/E332Y
-
site-directed mutagenesis
K121Q
the mutant is not associated with type 2 diabetes in African Americans
L49A/L50A
-
increase in cellular enzyme activity, redcution of activity in matrix vesicles
L50A
-
increase in cellular enzyme activity, reduction of activity in matrix vesicles
L60A
-
enzyme activity in matrix vesicles similar to wild-type
Y75G
-
enzyme activity in matrix vesicles similar to wild-type
D200N
mutation abolishes formation of the nucleotidylated intermediate
D358N
mutant enzyme can still form nucleotidylated catalytic intermediates but is hampered in the second step of catalysis
DELTA804-905
mutation results in complete loss of activity, protein remains entirely intracellular
F239A
mutation halves activity, decreased ability to trap the catalytic intermediate
F239Q
decreased activity and level of covalent intermediate of the mutant may be accounted for by a decreased binding of the substrate
H242L
60% decrease in enzymic acitivity
H242L/V246A
60% decrease in enzymic acitivity
H362Q
mutant enzyme can still form nucleotidylated catalytic intermediates but is hampered in the second step of catalysis
H406Q
mutation abolishes formation of the nucleotidylated intermediate
K173Q
polymorphisms of NPP1 is associated with the aetiology of insulin resistance, does not affect the dimerization or catalytic activity of NPP1 and does not endow NPP1 with an affinity for the insulin receptor
K237A
mutation halves activity
T238S
mutant enzyme can still form nucleotidylated catalytic intermediates but is hampered in the second step of catalysis
V246A
40% decrease in enzymic acitivity
E41Q/E42Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increase in the pyrophosphatase activity
E45Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increase in the pyrophosphatase activity
E61Q
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increase in the pyrophosphatase activity
K118A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increase in the pyrophosphatase activity
R97A/R98A
significant decrease in the nucleoside triphosphate pyrophosphohydrolase activity and concomitant increase in the pyrophosphatase activity
E199A
site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type
E199D
site-directed mutagenesis, the mutation doubles the enzyme activity against NAD(H)
F194S
site-directed mutagenesis, the mutation increases the relative enzyme activity against adenosine 5'-monophosphate-containing substrates, although the overall enzyme activity of the mutant enzyme decreases compared to the wild-type
H255A
site-directed mutagenesis, mutation of the highly conserved residue into an apolar increases enzyme activity against most phosphodiester substrates
N153A
site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type
N165A
site-directed mutagenesis, the mutant shows increased activity with substrate 4-nitrophenyl phosphate compared to the wild-type
T132A
site-directed mutagenesis, substitution of the highly conserved catalytic residue results in an inactive mutant
T132S
site-directed mutagenesis, substitution of the highly conserved catalytic residue results in an inactive mutant
additional information