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Literature summary extracted from

  • Krempl, C.; Lazzaretti, D.; Sprangers, R.
    A structural biology view on the enzymes involved in eukaryotic mRNA turnover (2023), Biol. Chem., 404, 1101-1121.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.59 crystal structure analysis, PDB ID 1VLR Mus musculus
3.6.1.59 crystal structure analysis, PDB ID 6GBS Thermochaetoides thermophila
3.6.1.59 crystal structure analysis, PDB IDs 5OSY, 3BL7, 3BL9 3BLA, 1ST0, 1ST4, 1XMM, 1XML, 4QDE, 4QDV, 4QEB Homo sapiens
3.6.1.59 crystal structure analysis, PDB IDs 6TRQ, 5BV3 Saccharomyces cerevisiae
3.6.1.62 structure analysis, PDB ID 4PMW Mus musculus
3.6.1.62 structure analysis, PDB IDs 2A6T, 2QKL, 2QKM, 3J3Y, 5KQ1, 5KQ4, 5N2V, 5J3T, 4A54, 4RO1 Schizosaccharomyces pombe
3.6.1.62 structure analysis, PDB IDs 5LON, 6AM0, 5LOP Kluyveromyces lactis
3.6.1.62 structure analysis, PDB IDs 5MP0, 5QOH-5QOZ, 5QP0-5QP9, 5QPA-5QPC, 6H25, 6D6Q, 6D6R Homo sapiens
3.6.1.62 structure analysis, PDB IDs 7TUV and 6MD3 Trypanosoma brucei
3.6.1.62 structure analysis, PDBIDs 2JVB, 4K6E, 4KG3, 4KG4, 5LM5, 5LMF, 5LMG, 6Y3Z, 2VNU, 2WP8, 5JEA, 5G06, 5K36, 4IFD, 5C0X, 5VZJ, 5C0W, 6FSZ, 6LQS Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Mus musculus
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Homo sapiens
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Saccharomyces cerevisiae
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Thermochaetoides thermophila
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Thermochaetoides thermophila DSM 1495
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Thermochaetoides thermophila CBS 144.50
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O Thermochaetoides thermophila IMI 039719
-
 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 additional information Mus musculus short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Homo sapiens short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Saccharomyces cerevisiae short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Thermochaetoides thermophila short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Thermochaetoides thermophila DSM 1495 short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Thermochaetoides thermophila CBS 144.50 short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.59 additional information Thermochaetoides thermophila IMI 039719 short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome ?
-
-
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Saccharomyces cerevisiae
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Homo sapiens
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Trypanosoma brucei
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Mus musculus
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Schizosaccharomyces pombe
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis CBS 2359
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Schizosaccharomyces pombe 972
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Schizosaccharomyces pombe ATCC 24843
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Saccharomyces cerevisiae ATCC 204508
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis ATCC 8585
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis DSM 70799
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis NBRC 1267
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis NRRL Y-1140
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O Kluyveromyces lactis WM37
-
 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.59 Homo sapiens Q96C86
-
-
3.6.1.59 Mus musculus Q9DAR7
-
-
3.6.1.59 Saccharomyces cerevisiae Q06151
-
-
3.6.1.59 Thermochaetoides thermophila G0S8A3 Thermochaetoides thermophila
-
3.6.1.59 Thermochaetoides thermophila CBS 144.50 G0S8A3 Thermochaetoides thermophila
-
3.6.1.59 Thermochaetoides thermophila DSM 1495 G0S8A3 Thermochaetoides thermophila
-
3.6.1.59 Thermochaetoides thermophila IMI 039719 G0S8A3 Thermochaetoides thermophila
-
3.6.1.62 Homo sapiens Q8IU60
-
-
3.6.1.62 Kluyveromyces lactis Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis ATCC 8585 Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis CBS 2359 Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis DSM 70799 Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis NBRC 1267 Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis NRRL Y-1140 Q6CIU1 Candida sphaerica
-
3.6.1.62 Kluyveromyces lactis WM37 Q6CIU1 Candida sphaerica
-
3.6.1.62 Mus musculus Q9CYC6
-
-
3.6.1.62 Saccharomyces cerevisiae P53550
-
-
3.6.1.62 Saccharomyces cerevisiae ATCC 204508 P53550
-
-
3.6.1.62 Schizosaccharomyces pombe O13828
-
-
3.6.1.62 Schizosaccharomyces pombe 972 O13828
-
-
3.6.1.62 Schizosaccharomyces pombe ATCC 24843 O13828
-
-
3.6.1.62 Trypanosoma brucei A0A3L6L8V4
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA] the enzyme undergoes a large structural change upon substrate recruitment, which results in the formation of one catalytically competent active site. At the same time, the other substrate binding site opens into an inactive conformation that allows for the concomitant recruitment of a second substrate. Upon hydrolysis of the first substrate, the N-terminal lid domain flips over to form a catalytically competent active site around the second substrate, and consequently releases the products from the first active site. These flipping motions become fast in the presence of a large excess of substrate, thereby inhibiting substrate turnover Mus musculus
a
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA] the enzyme undergoes a large structural change upon substrate recruitment, which results in the formation of one catalytically competent active site. At the same time, the other substrate binding site opens into an inactive conformation that allows for the concomitant recruitment of a second substrate. Upon hydrolysis of the first substrate, the N-terminal lid domain flips over to form a catalytically competent active site around the second substrate, and consequently releases the products from the first active site. These flipping motions become fast in the presence of a large excess of substrate, thereby inhibiting substrate turnover Homo sapiens
a
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA] the enzyme undergoes a large structural change upon substrate recruitment, which results in the formation of one catalytically competent active site. At the same time, the other substrate binding site opens into an inactive conformation that allows for the concomitant recruitment of a second substrate. Upon hydrolysis of the first substrate, the N-terminal lid domain flips over to form a catalytically competent active site around the second substrate, and consequently releases the products from the first active site. These flipping motions become fast in the presence of a large excess of substrate, thereby inhibiting substrate turnover Saccharomyces cerevisiae
a
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA] the enzyme undergoes a large structural change upon substrate recruitment, which results in the formation of one catalytically competent active site. At the same time, the other substrate binding site opens into an inactive conformation that allows for the concomitant recruitment of a second substrate. Upon hydrolysis of the first substrate, the N-terminal lid domain flips over to form a catalytically competent active site around the second substrate, and consequently releases the products from the first active site. These flipping motions become fast in the presence of a large excess of substrate, thereby inhibiting substrate turnover Thermochaetoides thermophila
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Mus musculus N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Homo sapiens N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Saccharomyces cerevisiae N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Thermochaetoides thermophila N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Thermochaetoides thermophila DSM 1495 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Thermochaetoides thermophila CBS 144.50 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Thermochaetoides thermophila IMI 039719 N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Mus musculus ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Homo sapiens ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Saccharomyces cerevisiae ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Thermochaetoides thermophila ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Mus musculus ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Homo sapiens ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Saccharomyces cerevisiae ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Thermochaetoides thermophila ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Thermochaetoides thermophila DSM 1495 ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Thermochaetoides thermophila DSM 1495 ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Thermochaetoides thermophila CBS 144.50 ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Thermochaetoides thermophila CBS 144.50 ?
-
-
3.6.1.59 additional information short 5'cap mRNA fragments (products of the exosomal degradation process, small capped RNA fragment of 2-5 nucleotides) are subsequently decapped by the scavenger decapping enzyme DcpS/Dcs1p, that releases m7GMP and the 5' diphosphorylated mRNA fragment. Interaction between DcpS and the exosome Thermochaetoides thermophila IMI 039719 ?
-
-
3.6.1.59 additional information enzyme DcpS is only active on very short mRNA fragments as longer mRNAs prevent the formation of the closed active site due to steric clashes between the enzyme and the third base in the substrate. Functionally, this elegant mechanism prevents the decapping of long mRNAs that might still be actively involved in translation Thermochaetoides thermophila IMI 039719 ?
-
-
3.6.1.59 S: a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
-
 Homo sapiens N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Saccharomyces cerevisiae N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Homo sapiens N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Trypanosoma brucei N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Mus musculus N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Schizosaccharomyces pombe N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis CBS 2359 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Schizosaccharomyces pombe 972 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Schizosaccharomyces pombe ATCC 24843 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Saccharomyces cerevisiae ATCC 204508 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis ATCC 8585 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis DSM 70799 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis NBRC 1267 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis NRRL Y-1140 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?
3.6.1.62 a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O
-
 Kluyveromyces lactis WM37 N7-methyl-GDP + a 5'-end phospho-ribonucleoside in mRNA + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.59 ? x * 80000, SDS-PAGE Mus musculus
3.6.1.59 ? x * 80000, SDS-PAGE Homo sapiens
3.6.1.59 ? x * 80000, SDS-PAGE Saccharomyces cerevisiae
3.6.1.59 ? x * 80000, SDS-PAGE Thermochaetoides thermophila
3.6.1.59 homodimer in the apo state, DcpS forms a symmetric homodimer with two active sites, each between the N- and C-terminal lobes Mus musculus
3.6.1.59 homodimer in the apo state, DcpS forms a symmetric homodimer with two active sites, each between the N- and C-terminal lobes Homo sapiens
3.6.1.59 homodimer in the apo state, DcpS forms a symmetric homodimer with two active sites, each between the N- and C-terminal lobes Saccharomyces cerevisiae
3.6.1.59 homodimer in the apo state, DcpS forms a symmetric homodimer with two active sites, each between the N- and C-terminal lobes Thermochaetoides thermophila

Synonyms

EC Number Synonyms Comment Organism
3.6.1.59 CTHT_0038110
-
 Thermochaetoides thermophila
3.6.1.59 Dcps
-
 Mus musculus
3.6.1.59 Dcps
-
 Homo sapiens
3.6.1.59 Dcps
-
 Saccharomyces cerevisiae
3.6.1.59 Dcps
-
 Thermochaetoides thermophila
3.6.1.59 Dcs1
-
 Saccharomyces cerevisiae
3.6.1.59 m7GpppX diphosphatase SwissProt Mus musculus
3.6.1.59 m7GpppX diphosphatase SwissProt Homo sapiens
3.6.1.59 m7GpppX diphosphatase SwissProt Saccharomyces cerevisiae
3.6.1.59 mRNA decapping enzyme
-
 Mus musculus
3.6.1.59 mRNA decapping enzyme
-
 Homo sapiens
3.6.1.59 mRNA decapping enzyme
-
 Saccharomyces cerevisiae
3.6.1.59 mRNA decapping enzyme
-
 Thermochaetoides thermophila
3.6.1.59 scavenger decapping enzyme
-
 Mus musculus
3.6.1.59 scavenger decapping enzyme
-
 Homo sapiens
3.6.1.59 scavenger decapping enzyme
-
 Saccharomyces cerevisiae
3.6.1.59 scavenger decapping enzyme
-
 Thermochaetoides thermophila
3.6.1.62 Dcp2
-
 Saccharomyces cerevisiae
3.6.1.62 Dcp2
-
 Homo sapiens
3.6.1.62 Dcp2
-
 Kluyveromyces lactis
3.6.1.62 Dcp2
-
 Trypanosoma brucei
3.6.1.62 Dcp2
-
 Mus musculus
3.6.1.62 Dcp2
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 Schizosaccharomyces pombe
3.6.1.62 m7GpppN-mRNA hydrolase SwissProt Saccharomyces cerevisiae
3.6.1.62 m7GpppN-mRNA hydrolase SwissProt Homo sapiens
3.6.1.62 m7GpppN-mRNA hydrolase SwissProt Schizosaccharomyces pombe
3.6.1.62 mRNA decapping complex subunit 2 SwissProt Schizosaccharomyces pombe
3.6.1.62 mRNA decapping enzyme
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 Saccharomyces cerevisiae
3.6.1.62 mRNA decapping enzyme
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 Homo sapiens
3.6.1.62 mRNA decapping enzyme
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 Kluyveromyces lactis
3.6.1.62 mRNA decapping enzyme
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 Trypanosoma brucei
3.6.1.62 mRNA decapping enzyme
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 Mus musculus
3.6.1.62 mRNA decapping enzyme
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 Schizosaccharomyces pombe

General Information

EC Number General Information Comment Organism
3.6.1.59 additional information the catalytic triad is H-x-H-x-H Homo sapiens
3.6.1.59 physiological function the enzyme DcpS is involved in mRNA decapping in 3'->5' mRNA decay. The decapping of a transcript results in an immediate inhibition of translation initiation and thus prevents the production of truncated proteins that can still occur in the 3'->5' degradation pathway Mus musculus
3.6.1.59 physiological function the enzyme DcpS is involved in mRNA decapping in 3'->5' mRNA decay. The decapping of a transcript results in an immediate inhibition of translation initiation and thus prevents the production of truncated proteins that can still occur in the 3'->5' degradation pathway Homo sapiens
3.6.1.59 physiological function the enzyme DcpS is involved in mRNA decapping in 3'->5' mRNA decay. The decapping of a transcript results in an immediate inhibition of translation initiation and thus prevents the production of truncated proteins that can still occur in the 3'->5' degradation pathway Saccharomyces cerevisiae
3.6.1.59 physiological function the enzyme DcpS is involved in mRNA decapping in 3'->5' mRNA decay. The decapping of a transcript results in an immediate inhibition of translation initiation and thus prevents the production of truncated proteins that can still occur in the 3'->5' degradation pathway Thermochaetoides thermophila
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Saccharomyces cerevisiae
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Homo sapiens
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Kluyveromyces lactis
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Trypanosoma brucei
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Mus musculus
3.6.1.62 physiological function the enzyme Dcp2 is involved in mRNA decapping in 5'->3' mRNA decay, mechanism, detailed overview Schizosaccharomyces pombe