Any feedback?
Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Pseudomonas aeruginosa
for references in articles please use BRENDA:EC2.7.7.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 α-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).
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
- 2.7.7.6
- chromatin
- histone
- rrna
- strand
-
rnaps
- nucleosome
- tata
- drosophila
-
pausing
- pre-mrnas
- tbp
-
nucleolar
- bacteriophage
-
polyadenylation
-
single-stranded
-
cyclin-dependent
-
holoenzyme
- cyclin
-
spacers
- helicase
-
fidelity
- polya
-
coactivator
-
protein-coding
-
transactivation
- adenovirus
- xenopus
- ribonucleoproteins
-
sequence-specific
-
stall
-
pause
-
chip-seq
- vaccinia
-
multisubunit
-
ribozyme
- heptapeptide
- duplex
-
h3k4me3
-
spliceosome
- nucleoplasm
-
run-on
-
supercoiled
-
trimethylation
-
subcomplexes
-
exonuclease
- heterochromatin
-
translesion
- medicine
- primase
- molecular biology
- analysis
- diagnostics
- drug development
-
misincorporation
-
proofread
- synthesis
showSynonyms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C RNA formation factors
-
-
-
-
chloroplast soluble RNA polymerase
-
-
-
-
deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
DNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
DNA-dependent RNA nucleotidyltransferase
-
-
-
-
DNA-dependent RNA polymerase
-
-
-
-
nucleotidyltransferase, ribonucleate
-
-
-
-
Pol II
-
-
-
-
ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleate polymerase
-
-
-
-
ribonucleic acid formation factors, C
-
-
-
-
ribonucleic acid nucleotidyltransferase
-
-
-
-
ribonucleic acid polymerase
-
-
-
-
ribonucleic acid transcriptase
-
-
-
-
ribonucleic polymerase
-
-
-
-
ribonucleic transcriptase
-
-
-
-
RNA formation factors, C
-
-
-
-
RNA nucleotidyltransferase
-
-
-
-
RNA nucleotidyltransferase (DNA-directed)
-
-
-
-
RNA polymerase
RNA polymerase I
-
-
-
-
RNA polymerase II
-
-
-
-
RNA polymerase III
-
-
-
-
RNA transcriptase
-
-
-
-
RNAP
RNAP I
-
-
-
-
RNAP II
-
-
-
-
RNAP III
-
-
-
-
transcriptase
-
-
-
-
RNA polymerase
-
-
-
-
RNAP
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9014-24-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Substrates: the enzyme is able to use a variety of DNA templates. DNA from bacteriphage phiPLS27 is transcribed more efficiently than DNA isolated from lamda or herring sperm. DNA isolated from bacteriophage T7 and T7 D111 is utilized more efficiently
Products: -
Products: -
?
additional information
?
-
-
Substrates: molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
Products: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: molecular mechanisms enabling sigma factor PvdS, directing the transcription of pyoverdine and virulence genes under iron limitation, to compete with the major sigma RpoD for RNA polymerase binding, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma-factors to the RNA polymerase RNAP core enzyme, regulation of RNAP holoenzyme, Esigma70, involving Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, which simultaneously interact with conserved region 2 and region 4 of sigma70 mediated by separate surfaces of Rsd, interaction with mutants of Rsd and AlgQ, mechanism, detailed overview. Rsd can strongly regulate the production of the Pseudomonas aeruginosa virulence factor pyocyanin in a manner that depends on their abilities to interact with sigma70 region 2
Products: -
Products: -
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
KCl, ZnCl2 and CaCl2 can not replace MgCl2 in the assay mixture
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
