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Literature summary extracted from

  • Peculis, B.A.; Reynolds, K.; Cleland, M.
    Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16) (2007), J. Biol. Chem., 282, 24792-24805.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.62
-
Xenopus laevis
3.6.1.62
-
Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.62 E150Q mutant protein is inactive under all conditions Xenopus laevis
3.6.1.62 E89Q mutant protein is inactive under all conditions Xenopus laevis
3.6.1.62 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
3.6.1.62 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
3.6.1.62 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

EC Number Inhibitors Comment Organism Structure
3.6.1.62 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.62 nucleolus
-
Xenopus laevis 5730
-
3.6.1.62 nucleolus
-
Homo sapiens 5730
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.62 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
3.6.1.62 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
3.6.1.62 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
3.6.1.62 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
3.6.1.62 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
3.6.1.62 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.62 30000
-
2 * 30000, SDS-PAGE Xenopus laevis
3.6.1.62 60000
-
gel filtration Xenopus laevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.62 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
-
?
3.6.1.62 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

EC Number Organism UniProt Comment Textmining
3.6.1.62 Homo sapiens Q96DE0
-
-
3.6.1.62 Xenopus laevis Q6TEC1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.62
-
Xenopus laevis
3.6.1.62
-
Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.62 ovary
-
Xenopus laevis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.62 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
-
?
3.6.1.62 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
-
?
3.6.1.62 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
-
?
3.6.1.62 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
-
?
3.6.1.62 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
-
?
3.6.1.62 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
-
?
3.6.1.62 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

EC Number Subunits Comment Organism
3.6.1.62 dimer 2 * 30000, SDS-PAGE Xenopus laevis

Synonyms

EC Number Synonyms Comment Organism
3.6.1.62 H29K
-
Homo sapiens
3.6.1.62 Nudt16
-
Homo sapiens
3.6.1.62 X29 protein
-
Xenopus laevis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.62 37
-
assay at Xenopus laevis
3.6.1.62 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.62 8.5
-
assay at Xenopus laevis
3.6.1.62 8.5
-
assay at Homo sapiens