Information on EC 3.6.1.59 - 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.59
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RECOMMENDED NAME
GeneOntology No.
5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] + H2O = N7-methylguanosine 5'-phosphate + a 5'-diphospho-[mRNA]
show the reaction diagram
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-dimethylguanosine 5'-[3-(5'-guanosinyl)-3-boranotriphosphate] + H2O
7-methylguanosine 5'-phosphate + ?
show the reaction diagram
7-methylguanosin-5'-yl-[3-(5'-guanosinyl)-2-boranotriphosphate] + H2O
7-methylguanosine 5'-phosphate + ?
show the reaction diagram
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
show the reaction diagram
7-methylguanosine 5'-diphosphate + nucleotidyl 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + ?
show the reaction diagram
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-
-
-
?
m7G5'ppp5'G + H2O
7-methylguanosine 5'-phosphate + ?
show the reaction diagram
-
-
-
?
m7G5'ppp5'G + H2O
7-methylguanosine 5'-phosphate + GDP
show the reaction diagram
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
show the reaction diagram
additional information
?
-
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Dcps shows no activity with 7-methylguanosine 5'-diphosphate
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7-methylguanosine 5'-diphosphate + H2O
7-methylguanosine 5'-phosphate + phosphate
show the reaction diagram
m7G5'ppp5'N(3'ppp5'N)n + H2O
7-methylguanosine 5'-phosphate + pp5'N(3'ppp5'N)n
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
C5-substituted quinazolines
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C5-quinazolines potently inhibit DcpS decapping activity. Binding of C5-substituted quinazolines to DcpS holds the enzyme in an open, catalytically incompetent conformation
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D156844
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highly effective at inhibiting recombinant DcpS decapping activity
Dcs2 protein
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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
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m7G5'ppp5'G
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00026
7-methylguanosine 5'-diphosphate
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pH 7.0, 30C, Dcs1 homodimer
0.00014
m7G5'ppp5'G
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pH 7.0, 30C, Dcs1 homodimer
additional information
additional information
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DcpS exhibits different enzymatic kinetics under low and high substrate conditions, negative cooperativity between two wild type subunits, reduced decapping activity is displayed by the DcpSWT/HIT heterodimer under high substrate conditions
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
7-methylguanosine 5'-diphosphate
Saccharomyces cerevisiae
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pH 7.0, 30C, Dcs1 homodimer
0.012
m7G5'ppp5'G
Saccharomyces cerevisiae
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pH 7.0, 30C, Dcs1 homodimer
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.5
7-methylguanosine 5'-diphosphate
Saccharomyces cerevisiae
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pH 7.0, 30C, Dcs1 homodimer
16632
86
m7G5'ppp5'G
Saccharomyces cerevisiae
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pH 7.0, 30C, Dcs1 homodimer
10339
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000015
D156844
Homo sapiens
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pH and temperature not specified in the publication
0.00003
m7G5'ppp5'G
Homo sapiens
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pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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DcpS is predominantly a nuclear protein, with low levels of in the cytoplasm
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37921
x * 37921, calculated from sequence
38600
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x * 38600, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at 20C. Structures of DcpS in ligand-free form and in a complex with m7GDP. Examination of the crystallographic B-factors indicates that the N-terminal domain in apo-DcpS is inherently flexible, and in a dynamic state ready for substrate binding and product release
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bisphosphonate mRNA cap analog attached to Sepharose for affinity chromatography of decapping enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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identification of DcpS as a candidate molecular target of the C5-substituted quinazolines for the potential treatment of spinal muscular atrophy