2.7.7.50: mRNA guanylyltransferase
This is an abbreviated version!
For detailed information about mRNA guanylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.50
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2.7.7.50
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cyclin
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photosystem
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thylakoids
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photoinhibition
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chloroplast
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cyanobacterium
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chlorophyll
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synechocystis
-
photodamage
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photochemical
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triphosphatase
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retinoblastoma
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cyclin-dependent
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vaccinia
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reinhardtii
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high-light
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photoprotection
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5'-triphosphatase
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qa
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mantle
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plastoquinone
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synechococcus
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oxygen-evolving
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thermoluminescence
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photoinactivation
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xanthophyl
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7-methylguanosine
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atrazine
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water-splitting
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p-tefb
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lhcii
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non-photochemical
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alpha-32pgtp
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water-oxidizing
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chloroplast-encoded
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biotechnology
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vp3
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diuron
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nsp1
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low-light
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lincomycin
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grana
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herbicide-resistant
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analysis
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psbo
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reoviridae
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cap-binding
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spt5
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photoinhibitory
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flash-induced
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uncapped
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thermosynechococcus
- 2.7.7.50
- cyclin
- photosystem
- thylakoids
-
photoinhibition
- chloroplast
- cyanobacterium
- chlorophyll
- synechocystis
-
photodamage
-
photochemical
- triphosphatase
- retinoblastoma
-
cyclin-dependent
- vaccinia
- reinhardtii
-
high-light
-
photoprotection
- 5'-triphosphatase
- qa
-
mantle
- plastoquinone
- synechococcus
-
oxygen-evolving
-
thermoluminescence
-
photoinactivation
-
xanthophyl
- 7-methylguanosine
- atrazine
-
water-splitting
- p-tefb
- lhcii
-
non-photochemical
-
alpha-32pgtp
-
water-oxidizing
-
chloroplast-encoded
- biotechnology
- vp3
- diuron
- nsp1
-
low-light
- lincomycin
-
grana
-
herbicide-resistant
- analysis
- psbo
- reoviridae
-
cap-binding
- spt5
-
photoinhibitory
-
flash-induced
-
uncapped
- thermosynechococcus
Reaction
Synonyms
A103R, A103R protein, cap guanylyltransferase-methyltransferase, capping enzyme, capping enzyme guanylyltransferase, Ceg1, CET1, CmCeg1, D1 protein, GDP polyribonucleotidyltransferase, GlCeg1, GTase, GTP-RNA guanylyltransferase, GTP:RNA GTase, guanylyltransferase, guanylyltransferase mRNA capping, HCE, L protein, Mce1, messenger RNA guanylyltransferase, More, mRNA capping enzyme, mRNA guanylyl transferase, mRNA-cap, mRNA-capping enzyme, NAD-decapping enzyme, nsP1, NudC, PRNTase, protein lambda2, RNA capping enzyme, RNA guanylyltransferase, RNGTT, TbCgm1, TTM-type RTPase-GTase, VACWR106, VP3
ECTree
2.7.7.50 mRNA guanylyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.7.7.50 - mRNA guanylyltransferase
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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
NAD-capped RNA + H2O
?
-
NudC is a single-strand-specific RNA-decapping enzyme with a strong preference for a purine as first nucleotide
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
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-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
-
-
-
-
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
ir
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
-
-
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
-
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
-
-
guanosine residue linked 5' through three 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
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
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
?
-
-
RNA polymerase II primary transcripts are substrates for the cellular capping enzyme
-
-
?
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
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-
?
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
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
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-
?
