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2'-fluoro-2'-deoxy-GTP + pp(5')RNA
2'-fluoro-2'-deoxy-G(5')ppp(5')RNA + diphosphate
0.16fold efficiency compared with substrate GTP
-
-
?
2-amino-6-chloropurine-beta-D-ribose triphosphate + pp(5')RNA
2-amino-6-chloropurine-beta-D-ribose-(5')ppp(5')RNA + diphosphate
0.08fold efficiency compared with substrate GTP
-
-
?
3'-deoxy-GTP + pp(5')RNA
3'-deoxy-G(5')ppp(5')RNA + diphosphate
0.15fold efficiency compared with substrate GTP
-
-
?
3'-O-methyl-GTP + mRNA
?
-
-
-
-
?
3'-O-methyl-GTP + pp(5')RNA
3'-O-methyl-G(5')ppp(5')RNA + diphosphate
0.38fold efficiency compared with substrate GTP
-
-
?
5'-NAD-capped RNA + ?
?
-
NudC is a single-strand-specific RNA-decapping enzyme with a strong preference for a purine as first nucleotide. NudC prefers NAD-RNA over NAD(H) by several orders of magnitude. The enzyme has strong preference for RNAs with at least three unpaired nucleotides at their 5' ends
-
-
?
6-methylthio-GTP + pp(5')RNA
6-methylthio-G(5')ppp(5')RNA + diphosphate
0.07fold efficiency compared with substrate GTP
-
-
?
6-thio-GTP + pp(5')RNA
6-thio-G(5')ppp(5')RNA + diphosphate
0.16fold efficiency compared with substrate GTP
-
-
?
8-bromo-GTP + pp(5')RNA
8-bromo-G(5')ppp(5')RNA + diphosphate
0.40fold efficiency compared with substrate GTP
-
-
?
8-iodoGTP + pp(5')RNA
8-iodo-G(5')ppp(5')RNA + diphosphate
1.0fold efficiency compared with substrate GTP
-
-
?
8-[(6-amino)hexyl]-amino-GTP-ATTO-680 + pp(5')RNA
G(5')ppp(5')RNA + diphosphate + ?
fluorescent substrate analog
-
-
?
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
GTP + (5')pp(5')-AACA(C/U)-mRNA
diphosphate + G(5')ppp(5')-AACA(C/U)-mRNA
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
GTP + diphosphate terminated poly(A) with an average chain length of 2000 nucleotides
?
-
-
-
-
?
GTP + diphosphate-ended poly(A)
?
-
-
-
-
?
GTP + lambdac17RNA
?
-
-
-
-
?
GTP + pp(5')A(pA)n
?
-
-
-
-
?
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
GTP + pp(5')GCC(A2,U2G)n
?
-
-
-
-
?
GTP + pp(5')GpCpC
G(5')ppp(5')GpCpC + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')GpXp
G(5')ppp(5')GpXp + diphosphate
bluetongue virus serotype 10
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
GTP + ppApG
G(5')ppp(5')ApG + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
GTP + ppp(5')ApGp
G(5')pppp(5')ApGp + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
GTP + pppGpCpC
G(5')pppp(5')GpCpC + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + termini of 5'-triphosphate poly(A)
?
-
-
-
-
?
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
N1-methyl-GTP + pp(5')RNA
N1-methyl-G(5')ppp(5')RNA + diphosphate
1.1fold efficiency compared with substrate GTP
-
-
?
NAD(H) + H2O
AMP + NMN(H)
-
c.f. 3.6.1.22. The enzyme is not very efficient in hydrolyzing NAD
-
-
?
NAD-capped RNA + H2O
?
-
NudC is a single-strand-specific RNA-decapping enzyme with a strong preference for a purine as first nucleotide
-
-
?
NTP + H2O
NDP + phosphate
-
-
-
-
?
O6-methyl-GTP + pp(5')RNA
O6-methyl-G(5')ppp(5')RNA + diphosphate
0.48fold efficiency compared with substrate GTP
-
-
?
pppG + ppp(5')A(pA)n
?
-
-
-
-
?
additional information
?
-
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
low activity
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
no activity
-
-
?
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
-
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
-
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + (5')pp(5')-AACA(C/U)-mRNA
diphosphate + G(5')ppp(5')-AACA(C/U)-mRNA
Lyssavirus rabies
-
the 5'-AAC sequence in the substrate RNAs is strictly essential for RNA capping with the L protein
-
-
?
GTP + (5')pp(5')-AACA(C/U)-mRNA
diphosphate + G(5')ppp(5')-AACA(C/U)-mRNA
Lyssavirus rabies RC-HL
-
the 5'-AAC sequence in the substrate RNAs is strictly essential for RNA capping with the L protein
-
-
?
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
-
-
-
-
?
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
-
-
-
-
?
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
-
-
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
-
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
active site structure, overview
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
-
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
-
-
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
-
two-step reaction, usage of a synthetic RNA substrate of 81 nucleotides from a PCR template encoding the 5' terminal portion of the PBCV-1 DNA polymerase gene, with a T7 RNA polymerase promoter, assay method development and evaluation, overview
-
-
r
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
-
-
-
-
ir
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
GMP is linked to the enzyme via a phosphoamide bond
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
bluetongue virus serotype 10
-
reversible formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
bluetongue virus serotype 10
-
GMP is linked to the enzyme via a phosphoamide bond
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse diphosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse diphosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse pyrophosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir, r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
reversible formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
GMP is linked to the enzyme via a phosphoamide bond
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
enzyme can transfer its bound GMP to GDP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
reversible formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
GMP is linked to the enzyme via a phosphoamide bond
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
enzyme can transfer its bound GMP to GDP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
the enzymes isolated guanylyltransferase domian, residues 211-597, is catalytically active in vitro
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
reversible formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
reversible formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
GMP is linked to the enzyme via a phosphoamide bond to the epsilon-amino group of Lys70
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
yeast RNA 5'-triphosphatase enzyme can be substituted by the enzyme of Candida albicans, but not by the human enzyme, to function in the capping enzyme complex together with the mRNA guanylyltransferase
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
molecular basis of substrate recognition by the RNA-capping enzyme
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is unmethylated vaccinia virus mRNA
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
no apparent base specificity for the penultimate nucleotide, a variety of synthetic homoribopolymers and naturally occuring mRNAs are effective substrates, vaccinia virus
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
only the alpha-phosphate is transferred
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
enzyme can modify synthetic poly(A) to form the structure m7G(5')ppp(5')AmP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
-
-
-
ir
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
-
-
-
ir
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
-
-
-
-
ir
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
ir
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
-
-
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
specifically requires 5'-triphosphate-terminated RNA chains
-
-
r
GTPgammaS + pp(5')RNA
?
-
no activity
-
-
?
GTPgammaS + pp(5')RNA
?
-
-
-
-
r
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
-
-
inosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
-
-
inosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
1.3fold efficiency compared with substrate GTP
-
-
?
additional information
?
-
the virus possesses a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase and guanine-N7 methyltransferase domains with a minimized tunnel fold and an active site strikingly similar to that of yeast Cet1. GTP:RNA GTase is the GTase component of MimiCE
-
-
?
additional information
?
-
detection of GTase activity by label transfer from radiolabeled GTP to the enzyme, formation of an SDS-stable about 75 kDa nucleotidyl-protein adduct
-
-
?
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
?
additional information
?
-
-
autoguanylylation
-
-
?
additional information
?
-
-
autoguanylylation
-
-
?
additional information
?
-
-
bifunctional enzyme catalyzing GTP methylation and subsequent transfer of the m7GMP moiety from m7GTP to the 5'-diphosphate end of viral RNA
-
-
?
additional information
?
-
bluetongue virus serotype 10
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
an RNAI mutant with a paired 5' end, as well as native Escherichia coli 5S rRNA (also possessing a paired 5' end) are resistant to enzyme processing
-
-
-
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
no activity with GDP
-
-
?
additional information
?
-
-
no activity with GDP
-
-
?
additional information
?
-
-
no activity with m7GTP
-
-
?
additional information
?
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
-
no donor: 7-methylGTP
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
?
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
?
additional information
?
-
-
mRNA capping enzyme
-
-
?
additional information
?
-
-
RNA polymerase II primary transcripts are substrates for the cellular capping enzyme
-
-
?
additional information
?
-
-
no activity with ATP
-
-
?
additional information
?
-
-
autoguanylylation
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
autoguanylylation
-
-
?
additional information
?
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
-
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
?
additional information
?
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
?
additional information
?
-
-
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
?
additional information
?
-
generation of RNAs harboring various different cap analogues. Cap-dependent translation can occur in the absence of theN7-methyl group on the cap structure provided that alternative modifications enable appropriate binding to eIF4E
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
mRNA capping enzyme
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
no acceptor: ppGp
-
-
?
additional information
?
-
-
in absence of acceptor RNA, the enzyme forms a nucleotidyl intermediate by phosphoamidate linkage of GMP
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
enzyme forms a covalent enzyme-GTP intermediate of apparent MW 45000
-
-
?
additional information
?
-
-
mRNA capping enzyme
-
-
?
additional information
?
-
RNA guanylyltransferase Ceg1 has dual specificity and interacts not only with Ser5P but also with Ser7P of the C-terminal domain of RNA polymerase II. Ser7 of the C-terminal domain is essential for the unconditional growth and efficient priming of the mRNA capping complex. Residues Arg159 and Arg185 of Ceg1 are the key residues that interact with the Ser5P, while Lys175 interacts with Ser7P of the C-terminal domain. These interactions appear to be in a specific pattern of Ser5PSer7PSer5P in a tri-heptad C-terminal domain (YSPTS(P)-PSYSPTSPS(P)YSPTS(P)PS)
-
-
?
additional information
?
-
-
RNA guanylyltransferase Ceg1 has dual specificity and interacts not only with Ser5P but also with Ser7P of the C-terminal domain of RNA polymerase II. Ser7 of the C-terminal domain is essential for the unconditional growth and efficient priming of the mRNA capping complex. Residues Arg159 and Arg185 of Ceg1 are the key residues that interact with the Ser5P, while Lys175 interacts with Ser7P of the C-terminal domain. These interactions appear to be in a specific pattern of Ser5PSer7PSer5P in a tri-heptad C-terminal domain (YSPTS(P)-PSYSPTSPS(P)YSPTS(P)PS)
-
-
?
additional information
?
-
-
the N-terminal of the enzyme promotes the recruitment of FACT (facilitates chromatin transcription that enhances the engagement of RNA polymerase II into transcriptional elongation) to the coding sequence of an active gene, ADH1, independently of mRNA capping activity. The absence of the N-terminal enzyme domain decreases FACT targeting to ADH1 and consequently reduces the engagement of RNA polymerase II in transcriptional elongation, leading to promoter-proximal accumulation of RNA polymerase II
-
-
-
additional information
?
-
-
the N-terminal of the enzyme promotes the recruitment of FACT (facilitates chromatin transcription that enhances the engagement of RNA polymerase II into transcriptional elongation) to the coding sequence of an active gene, ADH1, independently of mRNA capping activity. The absence of the N-terminal enzyme domain decreases FACT targeting to ADH1 and consequently reduces the engagement of RNA polymerase II in transcriptional elongation, leading to promoter-proximal accumulation of RNA polymerase II
-
-
-
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
little sequence specificity for RNA acceptor
-
-
?
additional information
?
-
-
no acceptor: RNA with a single 5'-terminal phosphate
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
-
-
?
additional information
?
-
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
-
-
?
additional information
?
-
-
no activity with GMP
-
-
?
additional information
?
-
-
no acceptor: RNA with 5'-hydroxyl terminus
-
-
?
additional information
?
-
-
no activity with GDP
-
-
?
additional information
?
-
-
lacks strict sequence specificity, homoribonucleotides containing purines are preferred, in presence of diphosphate the enzyme catalyzes the phosphorolysis of the dinucleoside triphosphate G(5')pp(5')A but not of m7(5')pp(5')A
-
-
?
additional information
?
-
-
no donor: 7-methylGTP
-
-
?
additional information
?
-
-
no acceptor: RNA with a single 5'-terminal phosphate
-
-
?
additional information
?
-
-
no acceptor: RNA with a single 5'-terminal phosphate
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
?
additional information
?
-
-
mRNA capping enzyme
-
-
?
additional information
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
-
-
?
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1.4
2'-fluoro-2'-deoxy-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.16
2-amino-6-chloropurine-ribose triphosphate
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.15
3'-deoxy-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.45
3'-O-Methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.1557
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
0.0026
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
0.0073
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
0.43
6-methylthio-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.22
6-thio-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
1.5
8-bromo-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.42
8-iodoGTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.1
GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.34
ITP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.08
N1-methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.15
O6-methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.0088
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
0.0069
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
0.0078
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
0.1557
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Yellow fever virus
37°C, pH not specified in the publication
0.1557
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Dengue virus
37°C, pH not specified in the publication
0.0026
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Yellow fever virus
37°C, pH not specified in the publication
0.0026
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Dengue virus
37°C, pH not specified in the publication
0.0073
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Yellow fever virus
37°C, pH not specified in the publication
0.0073
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Dengue virus
37°C, pH not specified in the publication
0.0088
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Yellow fever virus
37°C, pH not specified in the publication
0.0088
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Dengue virus
37°C, pH not specified in the publication
0.0069
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Yellow fever virus
37°C, pH not specified in the publication
0.0069
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Dengue virus
37°C, pH not specified in the publication
0.0078
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Yellow fever virus
37°C, pH not specified in the publication
0.0078
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Dengue virus
37°C, pH not specified in the publication
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D468A
site-directed mutagenesis, inactive mutant
K292A
site-directed mutagenesis, inactive mutant
K496A
site-directed mutagenesis, inactive mutant
K498A
site-directed mutagenesis, inactive mutant
H68A
-
mutation enhances GTP methylation reaction but disables the following transguanylation reaction
H68C
-
mutation results in a change in the nature nature of the bond linking the enzyme and m7GMP, suggesting that residue H68 covalently binds to m7GMP in the intermediate
P236A
-
the mutant shows 10% of wild type activity
R69A
-
the mutant shows high activity as compared to the wild type enzyme
E234A
mutation does not inhibit the formation of the phosphoamide intermediate
K177A
-
site-directed mutagenesis, no activity
K171A
-
site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
K190A
-
site-directed mutagenesis, autoguanylylation inactive
K197A
-
site-directed mutagenesis, 7.5% of wild-type autoguanylylation activity
K226A
-
site-directed mutagenesis, unaltered properties
K44A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K89A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K94A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K171A
-
site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
-
K190A
-
site-directed mutagenesis, autoguanylylation inactive
-
K44A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K89A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K94A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K175A
no loss of interaction with polymerase II C-terminal domain
K198A
no loss of interaction with polymerase II C-terminal domain
R159A
loss of interaction with polymerase II C-terminal domain. Residue Arg159 of Ceg1 interacts strongly with polymerase II C-terminal domain
R185A
loss of interaction with polymerase II C-terminal domain. Residue Arg185 of Ceg1 interacts strongly with polymerase II C-terminal domain
G164T
56ld increase in Kd value for Pol2 CTDSer5-PO4
G164T/H201N
349foldd increase in Kd value for Pol2 CTDSer5-PO4
H201N
46ld increase in Kd value for Pol2 CTDSer5-PO4
H201N/R364A/Y368F
98fold increase in Kd value for Pol2 CTDSer5-PO4
R157E
85fold increase in Kd value for Pol2 CTDSer5-PO4
R157E/H201N
526fold increase in Kd value for Pol2 CTDSer5-PO4
G164T
-
56ld increase in Kd value for Pol2 CTDSer5-PO4
-
G164T/H201N
-
349foldd increase in Kd value for Pol2 CTDSer5-PO4
-
H201N
-
46ld increase in Kd value for Pol2 CTDSer5-PO4
-
R157E
-
85fold increase in Kd value for Pol2 CTDSer5-PO4
-
R157E/H201N
-
526fold increase in Kd value for Pol2 CTDSer5-PO4
-
E192A
113% of wild-type guanylyltransferase activity, 4% of wild-type RNA triphosphatase activity
K478A
1% of wild-type guanylyltransferase activity, 42% of wild-type RNA triphosphatase activity
L47A/L50A/T51A
1% of wild-type guanylyltransferase activity, 43% of wild-type RNA triphosphatase activity
N181A
48% of wild-type guanylyltransferase activity, 69% of wild-type RNA triphosphatase activity
R186A
51% of wild-type guanylyltransferase activity, 92% of wild-type RNA triphosphatase activity
T10A
19% of wild-type guanylyltransferase activity, 104% of wild-type RNA triphosphatase activity
E192A
-
113% of wild-type guanylyltransferase activity, 4% of wild-type RNA triphosphatase activity
-
K478A
-
1% of wild-type guanylyltransferase activity, 42% of wild-type RNA triphosphatase activity
-
N181A
-
48% of wild-type guanylyltransferase activity, 69% of wild-type RNA triphosphatase activity
-
R186A
-
51% of wild-type guanylyltransferase activity, 92% of wild-type RNA triphosphatase activity
-
T10A
-
19% of wild-type guanylyltransferase activity, 104% of wild-type RNA triphosphatase activity
-
K294A
inactive, no functional complementation of the deficient Saccharomyces cerevisiae mutant
K294A
site-directed mutagenesis, no remaining guanylylation activity, no complementation of a deficient Saccharomyces mutant, RNA 5'-triphosphatase activity is retained
additional information
-
residues Y126, F144, F161, Y192, Y203, Y213, and W222, are critical for GTP methylation and S-adenosylmethionine binding during the GTP methylation reaction
additional information
residues 229567 comprise the minimum enzymatically active human guanylyltransferase domain
additional information
-
residues 229567 comprise the minimum enzymatically active human guanylyltransferase domain
additional information
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
additional information
-
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
additional information
-
RNA 5'-triphosphatase, CET1 or CES5, expressed from high copy number plasmid in Saccharomyces cerevisiae, can compensate the growth defect caused by mutation ceg1-25 of the RNA guanylyltransferase
additional information
-
expression of recombinant Candida albicans RNA 5'-triphosphatase GST-fusion protein in yeast RNA 5'-triphosphatase-deficient mutant cells binds to the guanylyltransferase of Saccharomyces cerevisiae and complements the growth defect of the mutant, while the human enzyme does not
additional information
-
CEG1 gene products with substitutions at Lys70 are unable to perform the reaction and support the viability in vivo
additional information
-
mutant consisting of the D1R domain, residues 1-545
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Myette J.R.; Niles E.G.
Characterization of the vaccinia virus RNA 5-triphosphatase and nucleoside triphosphate phosphohydrolase activities
J. Biol. Chem.
271
11945-11952
1996
Vaccinia virus
brenda
Martin, S.A.; Paoletti, E.; Moss, B.
Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions
J. Biol. Chem.
250
9322-9329
1975
Vaccinia virus, Vaccinia virus WR
brenda
Martin, S.A.; Moss, B.
Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions
J. Biol. Chem.
250
9330-9335
1975
Vaccinia virus
brenda
Ensinger, M.J.; Martin, S.A.; Paoletti, E.; Moss, B.
Modification of the 5-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus
Proc. Natl. Acad. Sci. USA
72
2525-2529
1975
Vaccinia virus
brenda
Martin, S.A.; Moss, B.
mRNA guanylyltransferase and mRNA (guanine-7-)-methyltransferase from vaccinia virions. Donor and acceptor substrate specificites
J. Biol. Chem.
251
7313-7321
1976
Vaccinia virus
brenda
Monroy, G.; Spencer, E.; Hurwitz, J.
Purification of mRNA guanylyltransferase from vaccinia virions
J. Biol. Chem.
253
4481-4489
1978
Vaccinia virus
brenda
Itho, N.; Yamada, H.; Kaziro, Y.; Mizumoto, K.
Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization
J. Biol. Chem.
262
1989-1995
1987
Saccharomyces cerevisiae
brenda
Groner, Y.; Aviv, H.
Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates
Biochemistry
17
977-982
1978
Homo sapiens
brenda
Shibagaki, Y.; Gilboa, E.; Itho, N.; Yamada, H.; Nagata, S.; Mizumoto, K.
mRNA capping enzyme. Isolation and characterization of the gene encoding mRNA guanylytransferase subunit from Saccharomyces cerevisiae
J. Biol. Chem.
267
9521-9528
1992
Saccharomyces cerevisiae
brenda
Shuman, S.; Hurwitz, J.
Capping enzyme
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
15
245-265
1982
Homo sapiens, Rattus norvegicus, Vaccinia virus
-
brenda
Dunigan, D.D.; Zaitlin, M.
Capping of tobacco mosaic virus RNA. Analysis of viral-coded guanylyltransferase-like activity
J. Biol. Chem.
265
7779-7786
1990
tobacco mosaic virus
brenda
Shuman, S.
Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in Escherichia coli
J. Biol. Chem.
265
11960-11966
1990
Vaccinia virus
brenda
Shuman, S.; Morham, S.G.
Domain structure of vaccinia virus mRNA capping enzyme. Activity of the Mr 95,000 subunit expressed in Escherichia coli
J. Biol. Chem.
265
11967-11972
1990
Vaccinia virus
brenda
Itoh, N.; Mizumoto, K.; Kaziro, Y.
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