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Literature summary extracted from

  • Terasaka, N.; Kimura, S.; Osawa, T.; Numata, T.; Suzuki, T.
    Biogenesis of 2-agmatinylcytidine catalyzed by the dual protein and RNA kinase TiaS (2011), Nat. Struct. Mol. Biol., 18, 1268-1274.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.22 C17A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 C17S complete loss of activity Archaeoglobus fulgidus
6.3.4.22 C210S complete loss of activity Archaeoglobus fulgidus
6.3.4.22 D11A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 D8A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 D9A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 E159A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 F286A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 F301A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 I143A reduced activity Archaeoglobus fulgidus
6.3.4.22 I49A reduced activity Archaeoglobus fulgidus
6.3.4.22 K52A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 N194A reduced activity Archaeoglobus fulgidus
6.3.4.22 N56A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 R217A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 R369A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 R44A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 R54A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 T18A complete loss of activity Archaeoglobus fulgidus
6.3.4.22 T18D complete loss of activity Archaeoglobus fulgidus
6.3.4.22 T53A complete loss of activity Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.4.22 alpha,beta-methyleneadenosine 5'-triphosphate
-
 Archaeoglobus fulgidus
6.3.4.22 beta,gamma-methyleneadenosine 5'-triphosphate
-
 Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.22 0.00029
-
 [tRNAIle2]-cytidine34 pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 0.00087
-
 agmatine pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 0.006
-
 ATP pH 8.8, 70°C Archaeoglobus fulgidus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.22 KCl optimal concentration: 100 mM Archaeoglobus fulgidus
6.3.4.22 Mg2+ optimal concentration: 2-5 mM Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.22 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

EC Number Organism UniProt Comment Textmining
6.3.4.22 Archaeoglobus fulgidus O28025
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.3.4.22 phosphoprotein the Thr18-Cyt34 kinase domain autophosphorylates the Thr18 of the enzyme Archaeoglobus fulgidus

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.22
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.22 ATP + agmatine + [tRNAIle2]-cytidine34 the enzyme catalyzes the essential modification at the anticodon wobble position (position 34) of the AUA-codon of tRNAIle Archaeoglobus fulgidus [tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
 ?
6.3.4.22 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 Archaeoglobus fulgidus [tRNAIle2]-2-agmatinylcytidine34 + AMP + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.4.22 TiaS
-
 Archaeoglobus fulgidus
6.3.4.22 tRNAIle-agm2C synthetase
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.22 70
-
 assay at Archaeoglobus fulgidus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.22 0.006
-
 agmatine pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 0.0062
-
 ATP pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 0.0065
-
 [tRNAIle2]-cytidine34 pH 8.8, 70°C Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.22 8.8
-
 assay at Archaeoglobus fulgidus

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.3.4.22 0.00037
-
 pH 8.8, 70°C Archaeoglobus fulgidus alpha,beta-methyleneadenosine 5'-triphosphate
6.3.4.22 0.00079
-
 pH 8.8, 70°C Archaeoglobus fulgidus beta,gamma-methyleneadenosine 5'-triphosphate

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.22 1
-
 ATP pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 6.9
-
 agmatine pH 8.8, 70°C Archaeoglobus fulgidus
6.3.4.22 22.41
-
 [tRNAIle2]-cytidine34 pH 8.8, 70°C Archaeoglobus fulgidus