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Literature summary for 2.7.7.50 extracted from
- Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain (2008), Structure, 16, 501-512.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| catalytically active native MimiCE-(1-237) protein by vapor diffusion against a precipitant solution containing PEG4000 plus citrate and acetate buffers, X-ray diffraction structure determination and analysis at 1.65-2.9 A resolution | Acanthamoeba polyphaga Mimivirus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D468A | site-directed mutagenesis, inactive mutant | Acanthamoeba polyphaga Mimivirus |
| K292A | site-directed mutagenesis, inactive mutant | Acanthamoeba polyphaga Mimivirus |
| K496A | site-directed mutagenesis, inactive mutant | Acanthamoeba polyphaga Mimivirus |
| K498A | site-directed mutagenesis, inactive mutant | Acanthamoeba polyphaga Mimivirus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Acanthamoeba polyphaga Mimivirus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | 30% of the activity with Mg2+ | Acanthamoeba polyphaga Mimivirus |  |
| Mg2+ | both reaction steps are dependent on divalent metal ions | Acanthamoeba polyphaga Mimivirus | |
| Mn2+ | 30% of the activity with Mg2+ | Acanthamoeba polyphaga Mimivirus | |
| additional information | Cd2+, Ca2+, and Zn2+ are less effective, no activity with Cu2+ | Acanthamoeba polyphaga Mimivirus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + (5')ppPur-mRNA | Acanthamoeba polyphaga Mimivirus | - |
diphosphate + G(5')pppPur-mRNA | - |
r | |
| additional information | Acanthamoeba polyphaga Mimivirus | the virus possesses a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase and guanine-N7 methyltransferase domains with a minimized tunnel fold and an active site strikingly similar to that of yeast Cet1. GTP:RNA GTase is the GTase component of MimiCE | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acanthamoeba polyphaga Mimivirus | Q5UQX1 | a giant virus of amoeba, e.g. isolated parasite of Acanthamoeba polyphaga | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA | GTP:RNA GTase, the GTase component of MimiCE, catalyzes a reversible two-step ping-pong reaction. The first step entails nucleophilic attack of the enzyme at the a phosphorus of GTP to form a covalent enzyme-(lysyl-N)-GMP intermediate plus pyrophosphate. In the second step, the beta-phosphate of 50 diphosphate-terminated RNA attacks the enzyme-GMP intermediate to form the GpppRNA cap and expel the lysine nucleophile | Acanthamoeba polyphaga Mimivirus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GTP + (5')ppPur-mRNA | - |
Acanthamoeba polyphaga Mimivirus | diphosphate + G(5')pppPur-mRNA | - |
r | |
| GTP + (5')ppPur-mRNA | active site structure, overview | Acanthamoeba polyphaga Mimivirus | diphosphate + G(5')pppPur-mRNA | - |
r | |
| additional information | the virus possesses a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase and guanine-N7 methyltransferase domains with a minimized tunnel fold and an active site strikingly similar to that of yeast Cet1. GTP:RNA GTase is the GTase component of MimiCE | Acanthamoeba polyphaga Mimivirus | ? | - |
? | |
| additional information | detection of GTase activity by label transfer from radiolabeled GTP to the enzyme, formation of an SDS-stable about 75 kDa nucleotidyl-protein adduct | Acanthamoeba polyphaga Mimivirus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain structure of capping enzymes, structure-function relationship, detailed overview | Acanthamoeba polyphaga Mimivirus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GTP:RNA GTase | - |
Acanthamoeba polyphaga Mimivirus |
| TTM-type RTPase-GTase | - |
Acanthamoeba polyphaga Mimivirus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Acanthamoeba polyphaga Mimivirus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8 | - |
Acanthamoeba polyphaga Mimivirus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 9.5 | 15% of maximal activity at pH 5.5, 45% at pH 9.5 | Acanthamoeba polyphaga Mimivirus |
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