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 (Engineering
Engineering on EC 2.7.7.50 - mRNA guanylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H68A
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mutation enhances GTP methylation reaction but disables the following transguanylation reaction
H68C
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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
E234A
mutation does not inhibit the formation of the phosphoamide intermediate
K171A
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site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
K197A
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site-directed mutagenesis, 7.5% of wild-type autoguanylylation activity
K44A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K89A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K94A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K171A
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site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
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K44A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
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K89A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
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K94A
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site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
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K294A
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/H201N
349foldd increase in Kd value for Pol2 CTDSer5-PO4
H201N/R364A/Y368F
98fold increase in Kd value for Pol2 CTDSer5-PO4
R157E/H201N
526fold increase in Kd value for Pol2 CTDSer5-PO4
G164T/H201N
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349foldd increase in Kd value for Pol2 CTDSer5-PO4
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R157E/H201N
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526fold increase in Kd value for Pol2 CTDSer5-PO4
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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
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113% of wild-type guanylyltransferase activity, 4% of wild-type RNA triphosphatase activity
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K478A
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1% of wild-type guanylyltransferase activity, 42% of wild-type RNA triphosphatase activity
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N181A
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48% of wild-type guanylyltransferase activity, 69% of wild-type RNA triphosphatase activity
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R186A
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51% of wild-type guanylyltransferase activity, 92% of wild-type RNA triphosphatase activity
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T10A
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19% of wild-type guanylyltransferase activity, 104% of wild-type RNA triphosphatase activity
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additional information
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
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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
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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
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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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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
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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
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CEG1 gene products with substitutions at Lys70 are unable to perform the reaction and support the viability in vivo
