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EC Tree
IUBMB Comments The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
The taxonomic range for the selected organisms is: Mus musculus The enzyme appears in selected viruses and cellular organisms
Synonyms
d1 protein, guanylyltransferase, capping enzyme, mrna capping enzyme, rna guanylyltransferase, mrna guanylyltransferase, prntase, rna capping enzyme, mrna-cap, mrna-capping enzyme,
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GTP-RNA guanylyltransferase
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messenger RNA guanylyltransferase
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RNA guanylyltransferase
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additional information
enzyme is part of the bifunctional capping enzyme, which consists of autonomous and non-overlapping RNA 5'-triphosphatase and a RNA guanylyltransferase domain and activity
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
guanylyltransferase domain: residues 211-597
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
conserved KXDG-motif
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
Lys294 is located in the active site in a KXDG-conserved motif
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nucleotidyl group transfer
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GTP:mRNA guanylyltransferase
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
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GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
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additional information
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GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
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guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
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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
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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
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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
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additional information
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enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
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additional information
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enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
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additional information
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phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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additional information
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phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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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
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GTP + (5')pp-mRNA
diphosphate + G(5')ppp-mRNA
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additional information
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additional information
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phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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additional information
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phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
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Mg2+
optimal at 5-10 mM
Mg2+
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred
Mn2+
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred
additional information
requirement for divalent cations
additional information
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requirement for divalent cations
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SwissProt
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mRNA capping enzyme
SwissProt
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MCE1_MOUSE
597
0
68684
Swiss-Prot
Mitochondrion (Reliability: 4 )
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28000
catalytically active residues 211-597, i.e. RNA guanylyltransferase domain, glycerol gradient sedimentation
46000
residues 1-210, i.e. RNA triphosphatase domain, glycerol gradient sedimentation
68000
mRNA capping enzyme, glycerol density gradient sedimentation
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monomer
1 * 46000, catalytically active residues 211-597, i.e. guanylyltransferase domain, + 1 * 28000, residues 1-210, i.e. RNA triphosphatase domain, SDS-PAGE
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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
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
additional information
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construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
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recombinant His-tagged full length enzyme as well as the recombinant His-tagged N-terminal and C-terminal domains from Escherichia coli BL21(DE3)
recombinant truncated mutant, residues 438-597, His-tagged
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DNA and amino acid sequence determination and analysis, expression of truncation mutant in Escherichia coli BL21(DE3) and wild-type and mutant K294A enzyme in Saccharomyces haploid deficient mutant strain, functional complementation of the latter by wild-type enzyme
expression of His-tagged full length enzyme, residues 211-597, comprising the catalytical domain, and residues 1-210 in Escherichia coli BL21(DE3)
expression of wild-type full length enzyme and catalytic domain in deficient Saccharomyces cerevisiae strain YBS2 as His-tagged protein, functional complementation by both of them
in vitro translation of wild-type and mutant enzyme
mRNA capping enzyme, DNA sequence determination and analysis
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Yue, Z.; Maldonado, E.; Pillutla, R.; Cho, H.; Reinberg, D.; Shatkin, A.J.
Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
Proc. Natl. Acad. Sci. USA
94
12898-12903
1997
Mus musculus (O55236), Mus musculus, Homo sapiens (O60942), Homo sapiens
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Ho, C.K.; Sriskanda, V.; McCracken, S.; Bentley, D.; Schwer, B.; Shuman, S.
The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
J. Biol. Chem.
273
9577-9585
1998
Mus musculus (O55236), Mus musculus
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Ramanathan, A.; Robb, G.; Chan, S.
mRNA capping Biological functions and applications
Nucleic Acids Res.
44
7511-7526
2016
Mus musculus
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