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Literature summary for 2.1.1.228 extracted from
- Kinetic analysis of tRNA methyltransferases (2015), Methods Enzymol., 560, 91-116 .
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays | Methanocaldococcus jannaschii | |
| additional information | - |
additional information | pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays | Haemophilus influenzae | |
| additional information | - |
additional information | pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays | Escherichia coli | |
| additional information | - |
additional information | pre-steady-state and steady-state Michaelis-Menten kinetics, single turnover assays | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Methanocaldococcus jannaschii |  |
| Mg2+ | required | Haemophilus influenzae | |
| Mg2+ | required | Escherichia coli | |
| Mg2+ | required | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Homo sapiens | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii NBRC 100440 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae RD | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii DSM 2661 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii ATCC 43067 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii JAL-1 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae DSM 11121 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae KW20 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Haemophilus influenzae ATCC 51907 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | Methanocaldococcus jannaschii JCM 10045 | - |
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A873 | - |
- |
| Haemophilus influenzae | P43912 | - |
- |
| Haemophilus influenzae ATCC 51907 | P43912 | - |
- |
| Haemophilus influenzae DSM 11121 | P43912 | - |
- |
| Haemophilus influenzae KW20 | P43912 | - |
- |
| Haemophilus influenzae RD | P43912 | - |
- |
| Homo sapiens | Q32P41 | - |
- |
| Methanocaldococcus jannaschii | Q58293 | i.e. Methanococcus jannaschii | - |
| Methanocaldococcus jannaschii ATCC 43067 | Q58293 | i.e. Methanococcus jannaschii | - |
| Methanocaldococcus jannaschii DSM 2661 | Q58293 | i.e. Methanococcus jannaschii | - |
| Methanocaldococcus jannaschii JAL-1 | Q58293 | i.e. Methanococcus jannaschii | - |
| Methanocaldococcus jannaschii JCM 10045 | Q58293 | i.e. Methanococcus jannaschii | - |
| Methanocaldococcus jannaschii NBRC 100440 | Q58293 | i.e. Methanococcus jannaschii | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Homo sapiens | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Haemophilus influenzae | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Escherichia coli | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii NBRC 100440 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Haemophilus influenzae RD | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii DSM 2661 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii ATCC 43067 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii JAL-1 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Haemophilus influenzae DSM 11121 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Haemophilus influenzae KW20 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the TrmD reaction is the chemistry of methyl transfer | Haemophilus influenzae ATCC 51907 | ? | - |
- |
|
| additional information | radioactive assay method development and evaluation using labeled S-adenosyl-L-methionine and unlabeled tRNA, detailed overview. The slow step of the Trm5 reaction is after methyl transfer and is associated with release of the m1G37-tRNA product | Methanocaldococcus jannaschii JCM 10045 | ? | - |
- |
|
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Homo sapiens | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii NBRC 100440 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae RD | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii DSM 2661 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii ATCC 43067 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii JAL-1 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae DSM 11121 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae KW20 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Haemophilus influenzae ATCC 51907 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
| S-adenosyl-L-methionine + guanine37 in tRNA | - |
Methanocaldococcus jannaschii JCM 10045 | S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EcTrmD | - |
Escherichia coli |
| HiTrmD | - |
Haemophilus influenzae |
| HsTrm5 | - |
Homo sapiens |
| MjTrm5 | - |
Methanocaldococcus jannaschii |
| TRM5 | - |
Methanocaldococcus jannaschii |
| TRM5 | - |
Homo sapiens |
| TrmD | - |
Haemophilus influenzae |
| TrmD | - |
Escherichia coli |
| TRMT5 | - |
Homo sapiens |
| tRNA methyltransferase | - |
Methanocaldococcus jannaschii |
| tRNA methyltransferase | - |
Haemophilus influenzae |
| tRNA methyltransferase | - |
Escherichia coli |
| tRNA methyltransferase | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Haemophilus influenzae |
| 37 | - |
assay at | Escherichia coli |
| 37 | - |
assay at | Homo sapiens |
| 55 | - |
assay at | Methanocaldococcus jannaschii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Methanocaldococcus jannaschii |
| 8 | - |
assay at | Haemophilus influenzae |
| 8 | - |
assay at | Escherichia coli |
| 8 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Methanocaldococcus jannaschii | |
| S-adenosyl-L-methionine | - |
Haemophilus influenzae | |
| S-adenosyl-L-methionine | - |
Escherichia coli | |
| S-adenosyl-L-methionine | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. Methanococcus jannaschii MjTrm5 is homologous to human Trm5 | Homo sapiens |
| evolution | at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. Trm5 belongs to the class I tRNA methyl transferases. Trm5 is an active monomer that uses the class I-fold. MjTrm5 is homologous to human Trm5 | Methanocaldococcus jannaschii |
| evolution | at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. EcTrmD is homologous to Haemophilus influenza TrmD | Escherichia coli |
| evolution | at least 5 classes (class I-V) of structurally distinct AdoMet-dependent methyltransferases have been identified. TrmD belongs to the class IV tRNA methyl transferases. TrmD is an obligated dimer that uses the class IV-fold for AdoMet binding. Escherichia coli EcTrmD is homologous to Haemophilus influenza TrmD | Haemophilus influenzae |
| additional information | evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview | Methanocaldococcus jannaschii |
| additional information | evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview | Haemophilus influenzae |
| additional information | evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview | Escherichia coli |
| additional information | evaluation of the kinetic assays that are used to reveal the distinction between TrmD and Trm5, overview | Homo sapiens |
| physiological function | methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome | Methanocaldococcus jannaschii |
| physiological function | methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome | Haemophilus influenzae |
| physiological function | methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome | Escherichia coli |
| physiological function | methylation is to the G37 base on the 3' side of the anticodon to generate m1G37-tRNA suppresses frameshift errors during protein synthesis and is therefore essential for cell growth in all three domains of life. This methylation is catalyzed by TrmD in bacteria and by Trm5 in eukaryotes and archaea. Although TrmD and Trm5 catalyze the same methylation reaction, kinetic analysis reveal that these two enzymes are unrelated to each other and are distinct in their reaction mechanism. Both TrmD and Trm5 are essential for cell growth, because their reaction product m1G37 occurring on the 3' side of the tRNA anticodon is necessary to suppress +1-frameshift errors on the ribosome | Homo sapiens |
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