Information on EC 2.7.7.88 - GDP polyribonucleotidyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.88
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RECOMMENDED NAME
GeneOntology No.
GDP polyribonucleotidyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5'-triphospho-mRNA + GDP = diphosphate + guanosine 5'-triphospho-mRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
5'-triphospho-mRNA:GDP 5'-phosphopolyribonucleotidyltransferase [G(5')ppp-mRNA-forming]
The enzyme from rhabdoviruses transfers 5'-monophosphorylated (p-)mRNA from 5'-triphosphorylated (ppp-)mRNA to GDP to form 5'-capped mRNA (GpppmRNA) in a viral mRNA-start sequence-dependent manner. The (p-)mRNA transfer reaction proceeds through a covalent enzyme-pmRNA intermediate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-triphospho-mRNA + GDP
diphosphate + guanosine 5'-triphospho-mRNA
show the reaction diagram
5'-triphospho-mRNA + GTP
diphosphate + guanosine 5'-tetraphospho-mRNA
show the reaction diagram
pppAACAG + GDP
diphosphate + guanosine 5'-pppAACAG |
show the reaction diagram
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oligo-RNa substrate. Residues G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E are essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP
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?
pppApApCpApG + GDP
diphosphate + guanosine 5'-pppApApCpApG
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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assay in presence of 1 mM divalent cation, Mn2+ is preferred over Mg2+
Mn2+
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assay in presence of 1 mM divalent cation, Mn2+ is preferred over Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
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inhibits formation of the enzyme-RNa complex
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H1217A
mutant is completely inactive in RNA capping
H1226A
no loss of activity
R1211A
mutant is completely inactive in RNA capping
R1218A
mutant is completely inactive in RNA capping
H1217A
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mutant is completely inactive in RNA capping
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H1226A
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no loss of activity
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R1211A
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mutant is completely inactive in RNA capping
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R1218A
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mutant is completely inactive in RNA capping
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F1285A
mutation abolishes RNA capping activity
G1112A
mutation abolishes RNA capping activity
H1241A
mutation abolishes RNA capping activity
Q1286A
mutation abolishes RNA capping activity
R1242A
mutation abolishes RNA capping activity
S1155A
about 10% of wild-type activity
S1168A
about 10% of wild-type activity
T1170A
mutation abolishes RNA capping activity
W1201A
mutation abolishes RNA capping activity
G1112A
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mutation abolishes RNA capping activity
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H1241A
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mutation abolishes RNA capping activity
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R1242A
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mutation abolishes RNA capping activity
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T1170A
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mutation abolishes RNA capping activity
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W1201A
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mutation abolishes RNA capping activity
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F1269A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
G1100A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
G1154A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
P1104A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
P1104V
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Q1270A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
T1157A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
T1157S
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
W1188A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Y1152A
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Y1152W
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residue is essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation and also reduces GTPase activity. Mutant induces termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolishes virus gene expression in host cells
Show AA Sequence (2027 entries)
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