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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Rattus norvegicus

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase
IUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
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Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase ii, pol ii, t7 rna polymerase, rna polymerase i, pol iii, rna polymerase iii, pol i, rnapii, rnap ii, dna-dependent rna polymerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C RNA formation factors
-
-
-
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chloroplast soluble RNA polymerase
-
-
-
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deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
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DNA-dependent ribonucleate nucleotidyltransferase
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-
-
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DNA-dependent RNA nucleotidyltransferase
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-
-
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DNA-dependent RNA polymerase
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-
-
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nucleotidyltransferase, ribonucleate
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-
-
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Pol II
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-
-
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ribonucleate nucleotidyltransferase
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-
-
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ribonucleate polymerase
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-
-
-
ribonucleic acid formation factors, C
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-
-
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ribonucleic acid nucleotidyltransferase
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-
-
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ribonucleic acid polymerase
-
-
-
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ribonucleic acid transcriptase
-
-
-
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ribonucleic polymerase
-
-
-
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ribonucleic transcriptase
-
-
-
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RNA formation factors, C
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-
-
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RNA nucleotidyltransferase
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-
-
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RNA nucleotidyltransferase (DNA-directed)
-
-
-
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RNA polymerase
-
-
-
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RNA polymerase I
-
-
-
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RNA polymerase II
RNA polymerase III
-
-
-
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RNA transcriptase
-
-
-
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RNAP
-
-
-
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RNAP I
-
-
-
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RNAP II
-
-
-
-
RNAP III
-
-
-
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transcriptase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
CAS REGISTRY NUMBER
COMMENTARY hide
9014-24-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cisplatin
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a single cisplatin 1,2-d(CG) intrastrand cross-link or a single cisplatin 1,3-d(GTG) intrastrand cross-link is a strong block to the enzyme. The efficiency of the block at a cisplatin 1,2-d(GG) intrastrand cross-link is similar in several different nucleotide sequence contexts. Some blockage is also observed when the single cisplatin 1,3-d(GTG) intrastrand cross-link is located in the non-transcribed strand. Cisplatin-induced lesions in the transcribed DNA strand constitute a strong physical barrier to RNA polymerase progression
RECQL5
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a DNA helicase of the RECQ family, directly inhibits RNA polymerase II. It RECQL5 inhibits both initiation and elongation in transcription assays reconstituted with highly purified general transcription factors and RNAPII, RECQL5 helicase activity is not required for inhibition
-
additional information
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no inhibition of RNA transcription by RECQL5 helicase-deficient point mutant RECQL5D157A, and another human RECQ family helicase, RECQL1
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPA2_RAT
1135
0
127721
Swiss-Prot
other Location (Reliability: 2)
RPA1_RAT
1716
0
194192
Swiss-Prot
Mitochondrion (Reliability: 4)
F1LM57_RAT
1135
0
128117
TrEMBL
other Location (Reliability: 2)
A0A8I5Y8F7_RAT
1131
0
127658
TrEMBL
Mitochondrion (Reliability: 2)
D3ZYB6_RAT
1205
0
136061
TrEMBL
Mitochondrion (Reliability: 2)
Q6LCR5_RAT
86
0
9655
TrEMBL
other Location (Reliability: 2)
G3V7B7_RAT
1716
0
194097
TrEMBL
Mitochondrion (Reliability: 4)
D4A5A6_RAT
1970
0
217206
TrEMBL
other Location (Reliability: 3)
E9PTB6_RAT
1303
0
146311
TrEMBL
other Location (Reliability: 2)
A0A8I6ASE2_RAT
1956
0
215767
TrEMBL
other Location (Reliability: 3)
G3V8Y5_RAT
1174
0
133897
TrEMBL
other Location (Reliability: 1)
Q5RK26_RAT
491
0
55076
TrEMBL
other Location (Reliability: 1)
D3ZV30_RAT
1133
0
127686
TrEMBL
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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RNA Pol II phosphorylation at Ser5 within the C-terminal domain
ubiquitination
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nondegradative ubiquitylation of RNA Pol II subunit Rpb1
additional information
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several posttranslational modifications of the large subunit of RNA polymerase II, Rpb1, including hydroxylation of Pro1465, nondegradative ubiquitylation of RNA Pol II, and phosphorylation of Ser5. Induction of Rpb1 hydroxylation, phosphorylation, and ubiquitylation requires the presence of the von Hippel-Lindau protein, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
nucleolar enzyme appears to be less stable than the nucleoplasmic enzyme, particularly in the presence of salt
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Weaver, R.F.; Blatti, S.P.; Rutter, W.J.
Molecular structures of DNA-dependent RNA polymerases (II) from calf thymus and rat liver
Proc. Natl. Acad. Sci. USA
68
2994-2999
1971
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Jacob, S.T.
Mammalian RNA polymerases
Prog. Nucleic Acid Res. Mol. Biol.
13
93-126
1973
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Tornaletti, S.; Patrick, S.M.; Turchi, J.J.; Hanawalt, P.C.
Behavior of T7 RNA polymerase and Mammalian RNA polymerase II at site-specific cisplatin adducts in the template DNA
J. Biol. Chem.
278
35791-35797
2003
Escherichia phage T7, Rattus norvegicus
Manually annotated by BRENDA team
Ayguen, O.; Xu, X.; Liu, Y.; Takahashi, H.; Kong, S.E.; Conaway, R.C.; Conaway, J.W.; Svejstrup, J.Q.
Direct inhibition of RNA polymerase II transcription by RECQL5
J. Biol. Chem.
284
23197-23203
2009
Rattus norvegicus
Manually annotated by BRENDA team
Ignacak, M.L.; Harbaugh, S.V.; Dayyat, E.; Row, B.W.; Gozal, D.; Czyzyk-Krzeska, M.F.
Intermittent hypoxia regulates RNA polymerase II in hippocampus and prefrontal cortex
Neuroscience
158
1436-1445
2009
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team