Information on EC 3.5.4.33 - tRNA(adenine34) deaminase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.5.4.33
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RECOMMENDED NAME
GeneOntology No.
tRNA(adenine34) deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenine34 in tRNA + H2O = hypoxanthine34 in tRNA + NH3
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
tRNA(adenine34) aminohydrolase
The enzyme is involved in editing of tRNA. The active site contains Zn2+ [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P47058: TAD2 and Q9URQ3: TAD3
P47058 and Q9URQ3
UniProt
Manually annotated by BRENDA team
P47058: TAD2 and Q9URQ3: TAD3
P47058 and Q9URQ3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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the wobble inosine tRNA modification is essential for cell cycle progression in the G1/S and G2/M transitions in fission yeast
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenine34 in tRNA + H2O
hypoxanthine34 in tRNA + NH3
show the reaction diagram
adenine34 in tRNAAla(AGC) + H2O
hypoxanthine34 in tRNAAla(IGC) + NH3
show the reaction diagram
adenine34 in tRNAArg + H2O
hypoxanthine34 in tRNAArg + NH3
show the reaction diagram
adenine34 in tRNAArg2 + H2O
hypoxanthine34 in tRNAArg2 + NH3
show the reaction diagram
adenine34 in tRNASer(AGA) + H2O
hypoxanthine34 in tRNASer(IGA) + NH3
show the reaction diagram
adenine34 in tRNAThr(AGU) + H2O
hypoxanthine34 in tRNAThr(IGU) + NH3
show the reaction diagram
adenine34 in tRNAVal + H2O
hypoxanthine34 in tRNAVal + NH3
show the reaction diagram
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?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenine34 in tRNA + H2O
hypoxanthine34 in tRNA + NH3
show the reaction diagram
adenine34 in tRNAArg + H2O
hypoxanthine34 in tRNAArg + NH3
show the reaction diagram
adenine34 in tRNAArg2 + H2O
hypoxanthine34 in tRNAArg2 + NH3
show the reaction diagram
O67050
the bacterial tRNA adenosine deaminase generates inosine by deaminating the adenosine residue at the wobble position of tRNAArg-2. This modification is essential for the decoding system
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?
adenine34 in tRNAThr(AGU) + H2O
hypoxanthine34 in tRNAThr(IGU) + NH3
show the reaction diagram
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?
adenine34 in tRNAVal + H2O
hypoxanthine34 in tRNAVal + NH3
show the reaction diagram
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-
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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optimum concentration2-5 mM, the enzyme does not require any cofactor, except magnesium ions, to deaminate adenosine 34 efficiently in tRNA. The dependence of the enzymatic reaction on magnesium ions probably reflects the need for a correct tRNA architecture
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5 mM abolishes activity up to 70%
4,7-phenanthroline
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5 mM abolishes activity up to 70%
additional information
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no inhibition by 2'-(8R)-deoxycoformycin up to 12 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000023
adenine34 in tRNASer(AGA)
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pH and temperature not specified in the publication
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0.00075 - 0.003
adenine34 in tRNAVal
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00083 - 0.0032
adenine34 in tRNAVal
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 4.3
adenine34 in tRNAVal
3581
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18718
2 * 18718, can form a homodimer in vitro, it is not proved that it is active as a homodimer in vitro, calculated from sequence
75000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tadA missing the last eight amino acids at the C-terminus is produced high-quality crystals, and the structure is determined at 1.6 A resolution, hanging drop vapor diffusion method
hanging drop vapor diffusion method, 1.8 A resolution. The large cavity formed around the catalytic site with the zinc ion seems to be important for accommodating the anticodon loop stem of tRNAArg-2
structure determination to 2.0 A of Staphylococcus aureus TadA bound to the anticodon stem-loop of tRNA(Arg2) bearing nebularine, a non-hydrolyzable adenosine analog, at the wobble position
crystal structure determined at 2.0 A resolution by multiwavelength anomalous dispersion using bound Zn2+
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crystallization at 22C by the sitting-drop method, in the presence of Zn2+ ion using ammonium sulfate as a precipitant. Flash-cooled crystals diffract to 2.0 A using 30% (v/v) glycerol as a cryoprotectant, crystal belongs to the tetragonal space group P4(2)2(1)2
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
N-terminally His6-tagged protein is expressed in Escherichia coli
overexpressed in Escherichia coli
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overexpression in Escherichi coli
overexpression in Escherichia coli
the C-terminal domain of Arabidopsis TADA (DN-TADA) is expressed in Escherichia coli fused to an N-terminal His tag
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F144A
mutations results in a reduction in enzymatic activity of about 800-fold
F145A
inactive mutant enzyme
R149A
mutations results in a reduction in enzymatic activity of about 800-fold
R94A
mutation substantially 220fold reduces the enzymatic activity
D64E
D64E abolishes the enzymatic activity of tadA in vitro, it does not detectably affect its activity in cells
C-terDELTA10
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mutation in subunit ADAT2, inactive mutant enzyme
C-terDELTA5
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mutation in subunit ADAT2, kcat/Km is 72% compared to the wild-type value
C136A
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kcat/Km is 13% of the wild-type value, mutation in subunit ADAT2
C136A/ADAT3 C291A
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inactive mutant enzyme, mutation in subunit ADAT2
C139A
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inactive mutant enzyme, mutation in subunit ADAT2
C291A
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inactive mutant enzyme, mutation in subunit ADAT3
C294A
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inactive mutant enzyme, mutation in subunit ADAT3
E92A/K216A/R217A/K218A/R219A
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inactive mutant enzyme
H252A
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inactive mutant enzyme, mutation in subunit ADAT3
H90A
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inactive mutant enzyme, mutation in subunit ADAT2
K216A
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mutation in subunit ADAT2, kcat/Km is 12% compared to the wild-type value
K218A
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mutation in subunit ADAT2, kcat/Km is 24% compared to the wild-type value
R217A
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mutation in subunit ADAT2, kcat/Km is 16% compared to the wild-type value
R219A
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mutation in subunit ADAT2, kcat/Km is 20% compared to the wild-type value
V254E
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inactive mutant enzyme, mutation in subunit ADAT3
V254L
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kcat/Km is 7% of the wild-type value, mutation in subunit ADAT3
V254T
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kcat/Km is 20% of the wild-type value, mutation in subunit ADAT3
additional information
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deletion of the last 10 amino acids at the C terminus of TbADAT2 abolishes tRNA binding. In addition, single alanine replacements of a string of positively charged amino acids (KRKRK) lead to binding defects that correlate with losses in enzyme activity
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