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3.1.3.5: 5'-nucleotidase

This is an abbreviated version!
For detailed information about 5'-nucleotidase, go to the full flat file.

Word Map on EC 3.1.3.5

Reaction

A 5'-ribonucleotide
+
H2O
=
a ribonucleoside
 +
phosphate

Synonyms

5'-adenylic phosphatase, 5'-AMP nucleotidase, 5'-AMPase, 5'-ectonucleotidase, 5'-mononucleotidase, 5'-NT, 5'-NT-1, 5'-NT-2, 5'-NT-3, 5'-NT-4, 5'-nucleotidase, 5'-nucleotidase A, 5'-nucleotidase I, 5'-nucleotidase II, 5'Nase, 5'nucleotidase, 5nA, 5NT, adenosine 5'-monophosphatase, adenosine 5'-phosphatase, adenosine monophosphatase, AMP phosphatase, AMP phosphohydrolase, AMP-selective 5'-nucleotidase, AMPase, c-N-I, c-N-II, Cant1, CD73, CD73 antigen, CD73/ecto-5'-nucleotidase, class C acid phosphatase, cN-I, cN-IA, cN-II, cN-III, cNI, cNII, cNIIIB nucleotidase, cytoplasmic 5'-nucleotidase II, cytoplasmic 5'-nucleotidase II (IMP-selective or GMP/IMP-selective), cytoplasmic 5'-nucleotidase III, cytoplasmic 5'-nucleotidase-I (AMP-selective), cytosolic 5'-nucleotidase, cytosolic 5'-nucleotidase II, cytosolic 5'-nucleotidase/phosphotransferase, E-5'-Nu, e-5NT, e-N, e5'-NT, e5'NT, ecto 5'-NT, ecto 5'-nucleotidase, ecto-5' nucleotidase, ecto-5'-NT, ecto-5'-NT/CD73, ecto-5'-nucleotidase, ecto-5'-nucleotidase/CD73, ecto-5'nucleotidase, ecto-5-NT, ecto-5-nucleotidase, ecto-nucleotidase, ectonuceotidase, ectonucleotidase, ectonucleotidase CD73, eN, eNs, eNT, GA-AMPase, high Km 5'-nucleotidase, high-Km 5'-NT, hppA gene product, IMP 5'-nucleotidase, IMP-GMP 5'-nucleotidase, IMP-GMP specific nucleotidase, IMP-specific, high Km 5'-nucleotidase, IMP/GMP selective 5'-NT, Isn1, membrane-bound 5'-nucleotidase, More, NMN 5'-nucleotidase, NT5C3A, NT5E, P5'N-1, Phm8, Pho5, PM-AMPase, PN-1, PN-I, purine 5'-NT, purine 5'-nucleotidase, pyrimidine 5'-nucleotidase, Sdt1, snake venom 5'-nucleotidase, soluble calcium-activated nucleotidase 1, thymidine monophosphate nucleotidase, type II cytosolic 5'-nucleotidase, UMPase, UMPH-1, uridine 5'-nucleotidase, uridine monophosphate hydrolase-1, UshA, XF_2089, YutF

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.5 5'-nucleotidase

Engineering

Engineering on EC 3.1.3.5 - 5'-nucleotidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42DELTAN
-
inactive mutant enzyme
D351E
-
strong decrease in nucleotidase activity, strong reduction in affinity towards Mg2+
D356E
-
strong decrease in nucleotidase activity, strong reduction in affinity towards Mg2+
D356N
-
strong increase in Km-value for inosine
D396A
site-directed mutagenesis, the mutant is only activable by 2,3-bisphosphoglycerate
D52A
-
inactive mutant enzyme
D52E
-
inactive mutant enzyme
D54A
-
inactive mutant enzyme
D54E
-
inactive mutant enzyme
F127E
site-directed mutagenesis
F36R
site-directed mutagenesis, inactive mutant
G319D
site-directed mutagenesis, the mutant shows altered kinetics compare to the wild-type enzyme
H428D
site-directed mutagenesis
I152D
site-directed mutagenesis
K292M
-
strong decrease in nucleotidase activity
K292R
-
strong decrease in nucleotidase activity
K311A
site-directed mutagenesis, the mutant shows altered kinetics compare to the wild-type enzyme
M436W
site-directed mutagenesis
M53I
-
lowest nucleotidase vs. phosphotransferase activity ratio of all mutants tested
M53N
-
strong decrease in catalytic efficiency
N154D
site-directed mutagenesis, the mutant shows a decrease in the value of K50 for Mg2+ compared to the wild-type enzyme
R144E
site-directed mutagenesis
S251A
-
kinetic behaviour almost similar to wild-type
S251T
-
kinetic behaviour almost similar to wild-type
T249S
-
kinetic behaviour almost similar to wild-type
T249V
-
strongly reduced enzyme activity
T56R
-
mutant devoid of phosphotransferase and nucleotidase activities
T56V
site-directed mutagenesis
Y115A
site-directed mutagenesis, the mutant behaves similar to the wild-type enzyme
Y55G
site-directed mutagenesis
D41N
-
specific activity of the mutant enzyme is 9.1% of the wild-type enzyme, activation by Co2+ is less than 2fold the level of activation of the wild-type enzyme
D84N
-
mutant enzyme exhibits 900fold decreased specific activity and increased level of activation by Co2+, 2700fold compared with approximately 40fold for the wild-type enzyme
E118Q
-
specific activity of the mutant enzyme is 6.1% of the wild-type enzyme, activation by Co2+ is 2.5fold the level of activation of the wild-type enzyme
H117N
-
specific activity of the mutant enzyme is 0.037% of the wild-type activity in presence of Co2+ and 0.042% of the wild-type activity in absence of Co2+
H217N
-
specific activity of the mutant enzyme is 0.23% of the wild-type enzyme. Activation by Co2+ is approximately 6fold the level of activation of the wild-type enzyme
H43N
-
specific activity of the mutant enzyme is 0.76% of the wild-type enzyme, activation by Co2+ is 4fold less than the activation of the wild-type enzyme
K191C/G398C
the mutations affect the enzyme activity
K191C/K532C
the mutations affect the enzyme activity
K191C/Q452C
the mutations affect the enzyme activity
P90C/L424C
enzyme variant that can adopt a closed and a half open conformation, active in oxidized state
S228C/P513C
enzyme variant trapped in open conformation, almost inactive, but up to 250fold activation by reduction of disulfide bridge
T124C/G398C
the mutations affect the enzyme activity
T124C/K532C
the mutations affect the enzyme activity
T124C/Q452C
the mutations affect the enzyme activity
D52N
site-directed mutagenesis, catalytically inactive active site residue
R86A
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is compromised
Y421S
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is compromised
Y421S/R86A
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is abolished
R86A
-
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is compromised
-
Y421S
-
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is compromised
-
Y421S/R86A
-
same level of basal activity as the wild-type for the substrate 4-nitrophenyl phosphate, but activation of 4-nitrophenyl phosphate hydrolysis by GTP is abolished
-
D51N
complete loss of activity
E96S
significant decrease in catalytic ability
H68A
significant decrease in catalytic ability
N69G
slightly higher Km compared to the wild?type
S117G
no significant changes compared to wild-type
T66G
no significant changes compared to wild-type
W113A
significant decrease in catalytic ability
Y114A
significant decrease in catalytic ability
F414A
the enzymatic activity of the mutant is significantly reduced compared to the wild type enzyme
R392A
the mutant shows very weak activity compared to the wild type enzyme
F414A
-
the enzymatic activity of the mutant is significantly reduced compared to the wild type enzyme
-
R392A
-
the mutant shows very weak activity compared to the wild type enzyme
-
additional information
-
individual expression of the N-terminal domain, amino acid residues Y26-V362, and the C-terminal domain, amino acid residues K363-Q550. The domains fold independently and properly. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate