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Literature summary for 2.7.7.52 extracted from
- Terminal uridylyl transferase of Vigna unguiculata: purification and characterization of an enzyme catalyzing the addition of a single UMP residue to the 3-end of an RNA primer (1981), Nucleic Acids Res., 9, 2433-2453.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| aurintricarboxylic acid | - |
Vigna unguiculata |  |
| Cibacron blue F3GA | - |
Vigna unguiculata | |
| diphosphate | - |
Vigna unguiculata | |
| heparin | - |
Vigna unguiculata | |
| Ionic strength | quite sensitive to ionic strength, activity decreases by 50% at about 40 mM (NH4)2SO4 or 125 mM potassium acetate | Vigna unguiculata | |
| additional information | not inhibitory: actinomycin C, rifamycin, alpha-amanitin, phosphate | Vigna unguiculata |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Vigna unguiculata | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | divalent cation required, Mg2+ or Mn2+, 4-12 mM stimulate, optimal at 5 mM | Vigna unguiculata | |
| Mn2+ | divalent cation required, Mg2+ or Mn2+, 1.1-1.5 mM stimulate | Vigna unguiculata | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50500 | - |
velocity sedimentation | Vigna unguiculata |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UTP + RNAn | Vigna unguiculata | RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate | diphosphate + RNAn+1 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Vigna unguiculata | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 614fold from uninfected and 117fold from CPMV-infected leaves | Vigna unguiculata |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Vigna unguiculata | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Vigna unguiculata |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UTP + RNAn | the enzyme requires a single-stranded oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as primer, e.g. oligoA20, tRNAAsp, E. coli RNA, alfalafa mosaic virus RNA 4 | Vigna unguiculata | diphosphate + RNAn+1 | - |
? | |
| UTP + RNAn | marked specificity for UTP | Vigna unguiculata | diphosphate + RNAn+1 | - |
? | |
| UTP + RNAn | RNA substrate specificity, overview | Vigna unguiculata | diphosphate + RNAn+1 | - |
? | |
| UTP + RNAn | RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate | Vigna unguiculata | diphosphate + RNAn+1 | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Vigna unguiculata |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
at least 3 h | Vigna unguiculata |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.2 | - |
assay at | Vigna unguiculata |
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