Information on EC 3.6.1.62 - 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.6.1.62
-
RECOMMENDED NAME
GeneOntology No.
5'-(N7-methylguanosine 5'-triphospho)-[mRNA] hydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 5'-(N7-methylguanosine 5'-triphospho)-[mRNA] + H2O = N7-methylguanosine 5'-diphosphate + a 5'-phospho-[mRNA]
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5'-(N7-methylguanosine 5'-triphospho)-[mRNA] N7-methylguanosine-5'-diphosphate phosphohydrolase
Decapping of mRNA is a critical step in eukaryotic mRNA turnover. The enzyme is unable to cleave a free cap structure (m7GpppG) [3]. The enzyme from Vaccinia virus is synergistically activated in the presence of Mg2+ and Mn2+ [5].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D10 decapping enzyme
-
-
D10 protein
-
-
D9 protein
-
-
decapping nudix hydrolase
-
hNUDT16
-
-
Nudt16
-
-
X29 protein
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
4-week-old C57BL/6 mice
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
no obvious phenotypic difference or differences in fertility, life span, or litter size are detected between the wild type animals and Dcp2b/b mice (mice containing a homozygous insertion of the beta-geo gene as Dcp2beta/beta)
malfunction
-
null mutants of DCP1 accumulate capped mRNAs with a reduced degradation rate. Lethal phenotype at the seedling cotyledon stage, with disorganized veins, swollen root hairs, and altered epidermal cell morphology
physiological function
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
physiological function
-
Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
physiological function
Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs; the presence or absence of detectable Dcp2 does not appreciably alter stability of the transfected RNA and suggests Dcp2 may not be involved in bulk mRNA decapping in cells. Dcp2 appears to be a minor contributor to mRNA stability and raises the intriguing possibility for the presence of a Dcp2-independent decapping activity in mammalian cells
physiological function
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
physiological function
-
the mRNA decapping activity of D10 allows Vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role. Although it may seem self-destructive for a virus to encode a decapping and a capping enzyme, accelerated mRNA turnover helps eliminate competing host mRNAs and allows stagespecific synthesis of viral proteins
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-(N7-methylguanosine 5'-triphospho)-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
luciferase mRNA
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. mRNA turnover mediated by the decapping complex is required for postembryonic development in Arabidopsis
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Dcp2 has role in mRNA decay
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Dcp2 is involved in mRNA decay
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
decapping of mRNA is a critical step in eukaryotic mRNA turnover
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
the mRNA decapping activity of D10 allows vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
a 60 nucleotide element at the 5' end of the mRNA encoding Rrp41 is preferentially bound and decapped by Dcp2. Enhanced decapping of this element is dependent on the structural integrity of its first 33 nt and not its primary sequence. The structure consists of a stem-loop positioned <10 nt from the 5' end of the mRNA
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
cleavage between the alpha- and beta-phosphates of the m7GpppN cap
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. Each component is required for mRNA decapping during postembryonic development
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Dcp2 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
decapping is specific for a methylated cap attached to RNA. D9 differs from D10 in requiring a longer capped RNA substrate for optimal activity. Only trace amounts of the 12- and 24-nt RNA substrates are cleaved. Higher activity with 36-, 48-, or 309-nt RNA substrates
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
hDcp2 is unable to cleave a free cap structure (m7GpppG) generated by P1 nuclease treatment of a cap-labelled RNA. Preferentially cleaves methylated cap structure
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
hDcp2-mediated decapping requires a functional Nudix (nucleotide diphosphate linked to an X moiety) pyrophosphatase motif
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
Nudt16 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Nudt16 can only function on capped RNA but not N7-methyl cap structure (m7GpppN)
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
RNAs of 24-309 nucleotides are decapped to comparable extents, whereas the cap of a 12-nt RNA is uncleaved. D10 recognizes its substrate through interaction with both cap and RNA moieties. The Nudix/MutT motif of VACV D10 is essential for RNA cap cleavage
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
the Dcp2 activity is mediated by the MutT/Nudix domain. A fragment of the yeast Dcp2 protein that contains the MutT/Nudix domain but lacks the non-conserved C-terminal tail is also active in decapping
-
?
m7G5'ppp5'-NO38 mRNA + H2O
m7GDP + 5'-phospho-NO38 mRNA
show the reaction diagram
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
-
?
m7G5'ppp5'-U3 snoRNA + H2O
m7GDP + 5'-phospho-U3 snoRNA
show the reaction diagram
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
-
?
m7G5'ppp5'-U3 snoRNA + H2O
m7GDP + U3 snoRNA + H2O
show the reaction diagram
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
-
?
m7G5'ppp5'-U8 snomRNA + H2O
m7GDP + 5'-phospho-U8 snomRNA
show the reaction diagram
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
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
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
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
-
?
additional information
?
-
-
X29 has decapping activity and releases m7GDP from full-length U8 RNA. The NUDIX domain in X29 is required for cap cleavage and release of m7GDP from U8 RNA. X29 can cleave the m227G cap present on U8 RNA in vivo
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
-
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
D9 is expressed early in infection and D10 late. It is suggested that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. mRNA turnover mediated by the decapping complex is required for postembryonic development in Arabidopsis
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
P53550
Dcp2 has role in mRNA decay
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Q8IU60
Dcp2 is involved in mRNA decay
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
decapping of mRNA is a critical step in eukaryotic mRNA turnover
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
mRNA decapping is a critical step in the control of mRNA stability and gene expression
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
Q6P3D0, Q9CYC6
regulation of RNA degradation plays an important role in the control of gene expression. Mammalian cells possess multiple mRNA decapping enzymes to regulate mRNA turnover. Nudt16, like Dcp2, is involved in mRNA stability. Each decapping enzyme can selectively affect the stability of at least a subset of mRNAs
-
?
m7G5'ppp5'-mRNA + H2O
m7GDP + 5'-phospho-mRNA
show the reaction diagram
-
the mRNA decapping activity of D10 allows vaccinia virus to accelerate degradation of viral and host messages. By degrading host mRNAs, VACV D10 may have an immunomodulatory role
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
Q6TEC1
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
?
m7G5'ppp5'-U8 snoRNA + H2O
m7GDP + 5'-phospho-U8 snoRNA
show the reaction diagram
Q96DE0
removes m7G and m227G caps from RNAs, rendering them substrates for 5'-3' exonucleases for degradation in vivo
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Co2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
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
Mg2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
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
Mn2+
-
hNUDT16 relies on divalent cations for its cap-hydrolysis activity to remove m7GDP and m227GDP from RNAs. hNUDT16 without the coordination of metals can not catalyze the hydrolytic reaction since no detectable cleaved products can be observed for either the U8 snoRNA or the mRNA substrate. Both Mg2+ and Mn2+ can effectively switch the protein from apoenzyme to holoenzyme. Mn2+ is more efficient as the activating factor
Zn2+
-
confer only limited hydrolytic capability on hNUDT16. After 30 min incubation of the RNA substrate with the enzyme, only tiny amounts of m7GDP product are observed on the migration profiles
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
supports D10p catalytic activity, but fails to demonstrate a synergistic effect on the enzyme when tested with Mn2+ ions
m7G5'ppp5'G
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
m7G5'ppp5'G
-
inhibits decapping at large molar ratios relative to capped RNA substrate
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
m7GDP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
m7GTP
-
inhibits decapping at large molar ratios relative to capped RNA substrate
Mg2+
-
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
N7-methylguanosine 5'-diphosphate
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
N7-methylguanosine 5'-triphosphate
-
D9 differs from D10 in having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA
poly(A) tail
-
presence of a poly(A) tail reduces the level of decapping by more than 2fold. The inhibition of decapping is reversed upon the addition of poly(A) competitor
-
uncapped RNA
-
D9 differs from D10 in having greater sensitivity to inhibition by uncapped RNA
-
uncapped RNA
-
high concentrations of uncapped RNA are inhibitory
-
Mn2+
-
presence of two metal-ion-binding sites on the enzyme. Synergistic activation of the enzyme in the presence of Mg2+ and Mn2+ ions, suggesting the existence of two metal-ion binding sites on the D10 protein. One metal ion is co-ordinated by Glu132, while the second metal ion is co-ordinated by Glu145
additional information
-
Ca2+ ions can not support D10p activity and does not produce a synergistic activation ofD10p in the presence of Mn2+
-
additional information
-
(m7GpppG) is unable to inhibit competitively the hDcp2 reaction
-
additional information
-
even higher concentrations of unmethylated analogs do not inhibit
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
VARICOSE protein
-
DCP2 interacts in vitro and in vivo with DCP1 and VARICOSE (VCS). The interacting proteins stimulate DCP2 activity, suggesting that the three proteins operate as a decapping complex. DCP1, DCP2, and VCS colocalize in cytoplasmic foci
-
DCP1 protein
-
DCP2 interacts in vitro and in vivo with DCP1 and VARICOSE (VCS). The interacting proteins stimulate DCP2 activity, suggesting that the three proteins operate as a decapping complex. DCP1, DCP2, and VCS colocalize in cytoplasmic foci
-
additional information
-
hDcp2 requires the presence of an mRNA body attached to the cap to be active
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
m7G5'ppp5'-mRNA
-
pH 7.5, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
m7G5'ppp5'G
Vaccinia virus
-
pH 7.5, 37C
0.3
m7GDP
Vaccinia virus
-
pH 7.5, 37C
0.003
m7GTP
Vaccinia virus
-
pH 7.5, 37C
0.003
uncapped RNA
Vaccinia virus
-
pH 7.5, 37C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
assay at
7.5
-
assay at
8
-
assay at
8
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
; Dcp2 is present in embryonic brain, heart, liver, and kidney. A substantial decrease of Dcp2 is evident in heart, liver, and kidney at birth and a continual decrease to undetectable levels in the adult; highest expression level. Dcp2 can be detected in the brain at all the developmental stages tested
Manually annotated by BRENDA team
; Dcp2 is present in embryonic brain, heart, liver, and kidney. A substantial decrease of Dcp2 is evident in heart, liver, and kidney at birth and a continual decrease to undetectable levels in the adult
Manually annotated by BRENDA team
; Dcp2 is present in embryonic brain, heart, liver, and kidney. A substantial decrease of Dcp2 is evident in heart, liver, and kidney at birth and a continual decrease to undetectable levels in the adult
Manually annotated by BRENDA team
; Dcp2 is present in embryonic brain, heart, liver, and kidney. A substantial decrease of Dcp2 is evident in heart, liver, and kidney at birth and a continual decrease to undetectable levels in the adult
Manually annotated by BRENDA team
; highest expression level
Manually annotated by BRENDA team
additional information
-
no activity in liver
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
primarily localized in cytoplasm
Manually annotated by BRENDA team
-
DCP1 and the interacting proteins, DCP2, and VCS colocalize in cytoplasmic foci
Manually annotated by BRENDA team
-
exclusively in the cytoplasm
Manually annotated by BRENDA team
-
hDcp2 is predominantly a nuclear protein, with low levels of in the cytoplasm
Manually annotated by BRENDA team
-
predominantly nucleolar
Manually annotated by BRENDA team
-
hDcp2 is predominantly a nuclear protein, with low levels of in the cytoplasm
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
-
gel filtration
715488
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 22000, SDS-PAGE
dimer
-
2 * 30000, SDS-PAGE
additional information
-
DCP2 and the interacting proteins DCP1, and VCS form a decapping complex in vivo. Each component is required for mRNA decapping during postembryonic development
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method
-
crystallizes as a homodimeric apoenzyme. Structure of X29 complexes with m7GpppA and pppG in the presence of Mn+2
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant D10 fusion protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expresiion in Escherichia coli
-
expression in Escherichia coli
-
overexpressed in Escherichia coli
-
expression of a fragment of the yeast Dcp2 protein in Escherichia coli. This fragment contains the MutT/Nudix domain but lacks the non-conserved C-terminal tail and is also active in decapping
(MBP)-D10 fusion is synthesized in Escherichia coli
-
cloned into a His-tagged expression vector, overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E148Q
-
mutant enzyme is as stable as the wild-type enzyme
E76Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
E79Q
-
mutation decreases the decapping activity of the enzyme
E80Q
-
mutation totally abolishes the decapping activity under the standard assaying condition
R75L
-
the mutant displays a weaker capability of hydrolysis
E132A
-
7.8% of wild-type activity. The E132A mutant shows a 5fold reduced affinity for Mg2+, but retains a Mn2+ affinity similar to that of the wild type
E141A
-
10% of wild-type activity. The E141A mutant demonstrates only slight variations in both Mg2+ and Mn2+ binding
E141Q
-
inactive mutant enzyme
E144Q/E145Q
-
inactive mutant enzyme
E150Q
-
mutant protein is inactive under all conditions
E89Q
-
mutant protein is inactive under all conditions
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
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
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
E145A
-
12.2% of wild-type activity. the E145A mutant shows 2-fold reduced affinity for Mg2+ and 6-fold reduced Mn2+ binding
additional information
-
decapping actiovity is abolished by point mutations in the Nudix hydrolase motif