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Literature summary for 3.6.1.62 extracted from
- Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16) (2007), J. Biol. Chem., 282, 24792-24805.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Xenopus laevis |
- |
Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E150Q | mutant protein is inactive under all conditions | Xenopus laevis |
| E89Q | mutant protein is inactive under all conditions | Xenopus laevis |
| E92Q | mutant displays weak decapping activity under the standard decapping conditions in both Mg2+ and Mn2+, a significant increase in hydrolysis in the presence of higher concentrations of metal | Xenopus laevis |
| E92Q/E93Q | mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis | Xenopus laevis |
| E93Q | mutation displays less than 5% decapping activity in Mn2+ under the optimized decapping conditions. A 10fold increase in the amount of metal present in the reaction (to 1 mM Mn2+) only marginally increases the efficiency of cap hydrolysis | Xenopus laevis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| m7GDP | although product inhibition by released m7GDP may occur, the amount of m7GDP released from RNA by X29 in these decapping reactions is well below the amount found to inhibit X29 decapping activity in the assay | Xenopus laevis |  |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| nucleolus | - |
Xenopus laevis | 5730 | - |
| nucleolus | - |
Homo sapiens | 5730 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher | Xenopus laevis | |
| Co2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher | Homo sapiens | |
| Mg2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Xenopus laevis | |
| Mg2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Homo sapiens | |
| Mn2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Xenopus laevis | |
| Mn2+ | the metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Homo sapiens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 30000 | - |
2 * 30000, SDS-PAGE | Xenopus laevis |
| 60000 | - |
gel filtration | Xenopus laevis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| m7G5'ppp5'-U8 snoRNA + H2O | Xenopus laevis | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
| m7G5'ppp5'-U8 snoRNA + H2O | Homo sapiens | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q96DE0 | - |
- |
| Xenopus laevis | Q6TEC1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Xenopus laevis |
- |
Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| ovary | - |
Xenopus laevis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| m7G5'ppp5'-NO38 mRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Xenopus laevis | m7GDP + 5'-phospho-NO38 mRNA | - |
? | |
| m7G5'ppp5'-U3 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Homo sapiens | m7GDP + 5'-phospho-U3 snoRNA | - |
? | |
| m7G5'ppp5'-U3 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Xenopus laevis | m7GDP + U3 snoRNA + H2O | - |
? | |
| m7G5'ppp5'-U8 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo | Xenopus laevis | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
| m7G5'ppp5'-U8 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo | Homo sapiens | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
| m7G5'ppp5'-U8 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Xenopus laevis | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
| m7G5'ppp5'-U8 snoRNA + H2O | removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo. The metal identity determines both the efficiency of decapping and the RNA substrate specificity. In Mg2+ the protein hydrolyzes the 5' cap from only one RNA substrate: U8 small nucleolar RNA. In the presence of Mn2+ or Co2+ all RNAs are substrates and the decapping efficiency is higher. The metal that binds the X29/H29K proteins in vivo may determine whether these decapping proteins function solely as a negative regulator of ribosome biogenesis or can decap a wider variety of nuclear-limited RNAs | Homo sapiens | m7GDP + 5'-phospho-U8 snoRNA | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 30000, SDS-PAGE | Xenopus laevis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| H29K | - |
Homo sapiens |
| Nudt16 | - |
Homo sapiens |
| X29 protein | - |
Xenopus laevis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Xenopus laevis |
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Xenopus laevis |
| 8.5 | - |
assay at | Homo sapiens |
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