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
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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
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Reaction
Reaction on EC 2.7.7.50 - mRNA guanylyltransferase
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active site
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
ATP/GTP-binding-site motif A, residues 379-386
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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
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
conserved KXDG-motif
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
conserved KXDG-motif
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active domain between residues 520 and 545, comprises both activities, the ATPase and guanylyltransferase activity
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
Lys294 is located in the active site in a KXDG-conserved motif
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mechanism of intermediate formation
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mechanism of capping
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mechanism of capping
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mechanism of capping
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active site Lys177
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active site Lys190
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
GTP:RNA GTase, the GTase component of MimiCE, catalyzes a reversible two-step ping-pong reaction. The first step entails nucleophilic attack of the enzyme at the a phosphorus of GTP to form a covalent enzyme-(lysyl-N)-GMP intermediate plus pyrophosphate. In the second step, the beta-phosphate of 50 diphosphate-terminated RNA attacks the enzyme-GMP intermediate to form the GpppRNA cap and expel the lysine nucleophile
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
RNA guanylyltransferase activity is involved in the synthesis of the cap structure found at the 5' end of eukaryotic mRNAs. The RNA guanylyltransferase activity is a two-step ping-pong reaction in which the enzyme first reacts with GTP to produce the enzyme-GMP covalent intermediate with the concomitant release of diphosphate. In the second step of the reaction, the GMP moiety is then transferred to a diphosphorylated RNA. Both reactions are reversible. The second step comprises the limiting steps for both the direct and reverse overall reactions
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
ATP/GTP-binding-site motif A, residues 379-386
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active site
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GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active site Lys190
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