BRENDA - Enzyme Database
show all sequences of 6.3.4.22

Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS

Terasaka, N.; Kimura, S.; Osawa, T.; Numata, T.; Suzuki, T.; Nat. Struct. Mol. Biol. 18, 1268-1274 (2011)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
C17A
complete loss of activity
Archaeoglobus fulgidus
C17S
complete loss of activity
Archaeoglobus fulgidus
C210S
complete loss of activity
Archaeoglobus fulgidus
D11A
complete loss of activity
Archaeoglobus fulgidus
D8A
complete loss of activity
Archaeoglobus fulgidus
D9A
complete loss of activity
Archaeoglobus fulgidus
E159A
complete loss of activity
Archaeoglobus fulgidus
F286A
complete loss of activity
Archaeoglobus fulgidus
F301A
complete loss of activity
Archaeoglobus fulgidus
I143A
reduced activity
Archaeoglobus fulgidus
I49A
reduced activity
Archaeoglobus fulgidus
K52A
complete loss of activity
Archaeoglobus fulgidus
N194A
reduced activity
Archaeoglobus fulgidus
N56A
complete loss of activity
Archaeoglobus fulgidus
R217A
complete loss of activity
Archaeoglobus fulgidus
R369A
complete loss of activity
Archaeoglobus fulgidus
R44A
complete loss of activity
Archaeoglobus fulgidus
R54A
complete loss of activity
Archaeoglobus fulgidus
T18A
complete loss of activity
Archaeoglobus fulgidus
T18D
complete loss of activity
Archaeoglobus fulgidus
T53A
complete loss of activity
Archaeoglobus fulgidus
Inhibitors
Inhibitors
Commentary
Organism
Structure
alpha,beta-methyleneadenosine 5'-triphosphate
-
Archaeoglobus fulgidus
beta,gamma-methyleneadenosine 5'-triphosphate
-
Archaeoglobus fulgidus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00029
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
0.00087
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
0.006
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
KCl
optimal concentration: 100 mM
Archaeoglobus fulgidus
Mg2+
optimal concentration: 2-5 mM
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + agmatine + [tRNAIle2]-cytidine34
Archaeoglobus fulgidus
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Archaeoglobus fulgidus
O28025
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
the Thr18-Cyt34 kinase domain autophosphorylates the Thr18 of the enzyme
Archaeoglobus fulgidus
Purification (Commentary)
Commentary
Organism
-
Archaeoglobus fulgidus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + agmatine + [tRNAIle2]-cytidine34
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
720531
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
-
?
ATP + agmatine + [tRNAIle2]-cytidine34
the precursor form of tRNAIle bearing an unmodified cytidine at the wobble position (C34) is aminoacylated with methionine (Met) and decodes the AUG codon.The Thr18-Cyt34 kinase domain first hydrolyzes ATP into AMP and diphosphate, then phosphorylates the C2 position of cytidine34 with the gamma-phosphate. Next, the amino group of agmatine attacks this position to release the phosphate and form 2-agmatinylcytidine. The Thr18-Cyt34 kinase domain also autophosphorylates the Thr18 of the enzyme, which may be involved in 2-agmatinylcytidine formation. Catalytic efficiency (kcat/Km) with GTP, UTP or CTP as substrate is less than 1% compared to ATP
720531
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Archaeoglobus fulgidus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.006
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
0.0062
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
0.0065
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at
Archaeoglobus fulgidus
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.00037
-
pH 8.8, 70°C
Archaeoglobus fulgidus
alpha,beta-methyleneadenosine 5'-triphosphate
0.00079
-
pH 8.8, 70°C
Archaeoglobus fulgidus
beta,gamma-methyleneadenosine 5'-triphosphate
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C17A
complete loss of activity
Archaeoglobus fulgidus
C17S
complete loss of activity
Archaeoglobus fulgidus
C210S
complete loss of activity
Archaeoglobus fulgidus
D11A
complete loss of activity
Archaeoglobus fulgidus
D8A
complete loss of activity
Archaeoglobus fulgidus
D9A
complete loss of activity
Archaeoglobus fulgidus
E159A
complete loss of activity
Archaeoglobus fulgidus
F286A
complete loss of activity
Archaeoglobus fulgidus
F301A
complete loss of activity
Archaeoglobus fulgidus
I143A
reduced activity
Archaeoglobus fulgidus
I49A
reduced activity
Archaeoglobus fulgidus
K52A
complete loss of activity
Archaeoglobus fulgidus
N194A
reduced activity
Archaeoglobus fulgidus
N56A
complete loss of activity
Archaeoglobus fulgidus
R217A
complete loss of activity
Archaeoglobus fulgidus
R369A
complete loss of activity
Archaeoglobus fulgidus
R44A
complete loss of activity
Archaeoglobus fulgidus
R54A
complete loss of activity
Archaeoglobus fulgidus
T18A
complete loss of activity
Archaeoglobus fulgidus
T18D
complete loss of activity
Archaeoglobus fulgidus
T53A
complete loss of activity
Archaeoglobus fulgidus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.00037
-
pH 8.8, 70°C
Archaeoglobus fulgidus
alpha,beta-methyleneadenosine 5'-triphosphate
0.00079
-
pH 8.8, 70°C
Archaeoglobus fulgidus
beta,gamma-methyleneadenosine 5'-triphosphate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
alpha,beta-methyleneadenosine 5'-triphosphate
-
Archaeoglobus fulgidus
beta,gamma-methyleneadenosine 5'-triphosphate
-
Archaeoglobus fulgidus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00029
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
0.00087
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
0.006
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
KCl
optimal concentration: 100 mM
Archaeoglobus fulgidus
Mg2+
optimal concentration: 2-5 mM
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + agmatine + [tRNAIle2]-cytidine34
Archaeoglobus fulgidus
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
the Thr18-Cyt34 kinase domain autophosphorylates the Thr18 of the enzyme
Archaeoglobus fulgidus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + agmatine + [tRNAIle2]-cytidine34
the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle
720531
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
-
?
ATP + agmatine + [tRNAIle2]-cytidine34
the precursor form of tRNAIle bearing an unmodified cytidine at the wobble position (C34) is aminoacylated with methionine (Met) and decodes the AUG codon.The Thr18-Cyt34 kinase domain first hydrolyzes ATP into AMP and diphosphate, then phosphorylates the C2 position of cytidine34 with the gamma-phosphate. Next, the amino group of agmatine attacks this position to release the phosphate and form 2-agmatinylcytidine. The Thr18-Cyt34 kinase domain also autophosphorylates the Thr18 of the enzyme, which may be involved in 2-agmatinylcytidine formation. Catalytic efficiency (kcat/Km) with GTP, UTP or CTP as substrate is less than 1% compared to ATP
720531
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Archaeoglobus fulgidus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.006
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
0.0062
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
0.0065
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.8
-
assay at
Archaeoglobus fulgidus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
6.9
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
22.41
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1
-
ATP
pH 8.8, 70°C
Archaeoglobus fulgidus
6.9
-
agmatine
pH 8.8, 70°C
Archaeoglobus fulgidus
22.41
-
[tRNAIle2]-cytidine34
pH 8.8, 70°C
Archaeoglobus fulgidus
Other publictions for EC 6.3.4.22
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
718503
Osawa
Crystallization and preliminar ...
Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
67
1414-1416
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
720531
Terasaka
Biogenesis of 2-agmatinylcytid ...
Archaeoglobus fulgidus
Nat. Struct. Mol. Biol.
18
1268-1274
2011
-
-
-
-
21
-
2
3
-
2
-
1
-
1
-
1
1
-
-
-
-
-
2
-
1
-
-
3
1
-
-
-
-
-
2
-
-
-
-
-
21
-
2
2
-
3
-
2
-
1
-
-
1
1
-
-
-
-
2
-
1
-
-
3
1
-
-
-
-
-
-
-
3
3
720532
Osawa
Structural basis of tRNA agmat ...
Archaeoglobus fulgidus
Nat. Struct. Mol. Biol.
18
1275-1280
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
705848
Ikeuchi
Agmatine-conjugated cytidine i ...
Archaeoglobus fulgidus, Pyrococcus horikoshii
Nat. Chem. Biol.
6
277-282
2010
-
-
1
-
7
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
7
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-