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Information on EC 3.6.1.59 - 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q06151
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3.6.1.59 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphataseIUBMB Comments
The enzyme removes (decaps) the N7-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides [3,6]. Decapping is an important process in the control of eukaryotic mRNA degradation. The enzyme functions to clear the cell of cap structure following decay of the RNA body . The nematode enzyme can also decap triply methylated substrates, 5'-(N2,N2,N7-trimethyl 5'-triphosphoguanosine)-[mRNA] .
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Word Map
- 3.6.1.59
- heterodimer
- m7gdp
- disability
- nucleoside
-
hint
-
exosome
-
diauxie
-
craniofacial
- trehalase
-
exonucleolytic
-
intellectual
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
scavenger mrna decapping enzyme, ylr270w, ydcps, m7gpppx pyrophosphatase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] N7-methylguanosine 5'-phosphate phosphohydrolase
The enzyme removes (decaps) the N7-methylguanosine 5-phosphate cap from an mRNA degraded to a maximal length of 10 nucleotides [3,6]. Decapping is an important process in the control of eukaryotic mRNA degradation. The enzyme functions to clear the cell of cap structure following decay of the RNA body [2]. The nematode enzyme can also decap triply methylated substrates, 5'-(N2,N2,N7-trimethyl 5'-triphosphoguanosine)-[mRNA] [4].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7-methylguanosine 5'-diphosphate + nucleotidyl 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + ?
-
-
-
?
5'-[GpppA]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[GpppC]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[GpppG]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[GpppU]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7AraGpppA]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7AraGpppC]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7AraGpppG]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7AraGpppU]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7dGpppA]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7dGpppC]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7dGpppG]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7dGpppU]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GppPAm]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppA]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppCm]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppC]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppGm]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppG]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7Gpppm6Am]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7Gpppm6A]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppUm]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7GpppU]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
5'-[m7Gppp]GUAGAACUUCGUCGAGUACGCUCAA[FAM]-3' + H2O
?
-
the substrate is 95% decapped at 0.0027 mM enzyme
-
-
?
a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
the enzyme decaps RNA transcripts as long as 1400 nucleotides
-
-
?
additional information
?
-
-
the enzyme can decap most guanosine caps. In contrast, it shows no activity towards adenosine, cytidine or uridine capped RNAs
-
-
-
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
-
-
-
?
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
cleavage of 7-methylguanosine 5'-diphosphate generated by Dcp1/Dcp2-mediated decapping in the 5' to 3' decay pathway
-
-
?
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
mRNA degradation occurs through distinct pathways, one primarily from the 5' end of the mRNA and the second from the 3' end. Decay from the 3' end generates the m7G5'ppp5'N cap dinucleotide, which is subsequently hydrolyzed to m7Gp and nucleotidyl 5'-diphosphate in Saccharomyces cerevisiae by a scavenger decapping activity termed Dcs1p
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
cleavage of 5' end m7G-oligoribonucleotide fragments generated by 3' to 5' exonucleolytic decay
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
n = 1-8
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
n = 1-8, mRNA degradation occurs through distinct pathways, one primarily from the 5' end of the mRNA and the second from the 3' end. Decay from the 3' end generates the m7GpppN cap dinucleotide, which is subsequently hydrolyzed to m7Gp and ppN in Saccharomyces cerevisiae by a scavenger decapping activity termed Dcs1p
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O
N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
-
the enzyme decaps RNA transcripts as long as 1400 nucleotides
-
-
?
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
cleavage of 7-methylguanosine 5'-diphosphate generated by Dcp1/Dcp2-mediated decapping in the 5' to 3' decay pathway
-
-
?
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
mRNA degradation occurs through distinct pathways, one primarily from the 5' end of the mRNA and the second from the 3' end. Decay from the 3' end generates the m7G5'ppp5'N cap dinucleotide, which is subsequently hydrolyzed to m7Gp and nucleotidyl 5'-diphosphate in Saccharomyces cerevisiae by a scavenger decapping activity termed Dcs1p
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
cleavage of 5' end m7G-oligoribonucleotide fragments generated by 3' to 5' exonucleolytic decay
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
n = 1-8
-
-
?
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
n = 1-8, mRNA degradation occurs through distinct pathways, one primarily from the 5' end of the mRNA and the second from the 3' end. Decay from the 3' end generates the m7GpppN cap dinucleotide, which is subsequently hydrolyzed to m7Gp and ppN in Saccharomyces cerevisiae by a scavenger decapping activity termed Dcs1p
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is independent of divalent metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dcs2 protein
Dcs2 is recruited into cytoplasmic P bodies, its inhibitory function may be focused in these centres of mRNA storage/turnover. Dcs2 is a stress-induced regulatory protein that modulates m7GpppX pyrophosphatase activity
-
KCl
-
the decapping reaction is significantly inhibited by increasing salt concentration, with KCl being a more potent inhibitor than NaCl
NaCl
-
the decapping reaction is significantly inhibited by increasing salt concentration, with KCl being a more potent inhibitor than NaCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00026
7-methylguanosine 5'-diphosphate
pH 7.0, 30°C, Dcs1 homodimer
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
7-methylguanosine 5'-diphosphate
pH 7.0, 30°C, Dcs1 homodimer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.5
7-methylguanosine 5'-diphosphate
pH 7.0, 30°C, Dcs1 homodimer
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
depletion of Dcs1, reduces chronological life span, possibly by modulating m7G misincorporation into nucleic acids. This can potentially link control of mRNA metabolism with senescence
malfunction
disruption of the DCS1 gene manifests a threefold increase of the TIF51A mRNA half-life. 5' to 3' exoribonucleolytic activity is impeded in the dcs1DELTAstrain, resulting in the accumulation of uncapped mRNA
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
Dcs1 is active as a homodimer. Dcs2 protein forms a heterodimer together with Dcs1, both modulating Dcs1 substrate specificity and suppressing its turnover number
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malys, N.; McCarthy, J.E.
Dcs2, a novel stress-induced modulator of m7GpppX pyrophosphatase activity that locates to P bodies
J. Mol. Biol.
363
370-382
2006
Saccharomyces cerevisiae (Q06151), Saccharomyces cerevisiae
Liu, H.; Rodgers, N.D.; Jiao, X.; Kiledjian, M.
The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
EMBO J.
21
4699-4708
2002
Saccharomyces cerevisiae (Q06151), Homo sapiens (Q96C86)
Liu, H.; Kiledjian, M.
Scavenger decapping activity facilitates 5' to 3' mRNA decay
Mol. Cell. Biol.
25
9764-9772
2005
Saccharomyces cerevisiae (Q06151)
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