BRENDA - Enzyme Database

Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea

Ikeuchi, Y.; Kimura, S.; Numata, T.; Nakamura, D.; Yokogawa, T.; Ogata, T.; Wada, T.; Suzuki, T.; Suzuki, T.; Nat. Chem. Biol. 6, 277-282 (2010)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
6.3.4.22
expression in Escherichia coli
Archaeoglobus fulgidus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
6.3.4.22
C352A/C355A
almost no 2-agmatinylcytidine formation is observed
Archaeoglobus fulgidus
6.3.4.22
G218A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
R140/G141A
mutation completely abolishes activity
Archaeoglobus fulgidus
6.3.4.22
R164A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
R217A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
T248A/D249A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
Y163A
mutation reduces activity
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
Archaeoglobus fulgidus
-
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.3.4.22
Archaeoglobus fulgidus
O28025
-
-
6.3.4.22
Pyrococcus horikoshii
O59476
-
-
Purification (Commentary)
EC Number
Commentary
Organism
6.3.4.22
-
Archaeoglobus fulgidus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
-
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
?
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Pyrococcus horikoshii
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
-
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.4.22
expression in Escherichia coli
Archaeoglobus fulgidus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
6.3.4.22
C352A/C355A
almost no 2-agmatinylcytidine formation is observed
Archaeoglobus fulgidus
6.3.4.22
G218A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
R140/G141A
mutation completely abolishes activity
Archaeoglobus fulgidus
6.3.4.22
R164A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
R217A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
T248A/D249A
mutation reduces activity
Archaeoglobus fulgidus
6.3.4.22
Y163A
mutation reduces activity
Archaeoglobus fulgidus
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
Archaeoglobus fulgidus
-
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.4.22
-
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
-
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Archaeoglobus fulgidus
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
?
6.3.4.22
ATP + agmatine + [tRNAIle2]-cytidine34
-
705848
Pyrococcus horikoshii
[tRNAIle2]-2-agmatinylcytidine34 + ?
-
-
-
-
General Information
EC Number
General Information
Commentary
Organism
6.3.4.22
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
Archaeoglobus fulgidus
6.3.4.22
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
Pyrococcus horikoshii
General Information (protein specific)
EC Number
General Information
Commentary
Organism
6.3.4.22
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
Archaeoglobus fulgidus
6.3.4.22
physiological function
modification at the anticodon wobble position of archaeal tRNAIle2. According to the chemical structure of agm2C, conjugation of an agmatine moiety at the C2 position of cytosine induces a tautomeric conversion with protonation of the N3 position and imino group formation at the C4 position. This modification completely alters the proton donor-acceptor pattern of cytosine in Watson-Click hydrogen bonding to that of uracil, enabling agm2C to base pair with adenine instead of guanine. tRNAIle2 acquires the ability to decode the AUA codon via formation 2-agmatinylcytidine
Pyrococcus horikoshii