Information on EC 2.7.7.19 - polynucleotide adenylyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.7.19
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RECOMMENDED NAME
GeneOntology No.
polynucleotide adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + RNAn = diphosphate + RNAn+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:polynucleotide adenylyltransferase
Also acts slowly with CTP. Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-30-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
two isoforms
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain CB15, enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
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Manually annotated by BRENDA team
strain CB15, enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
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Manually annotated by BRENDA team
Coturnix sp.
Quail
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Manually annotated by BRENDA team
CHO fibroblasts
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Manually annotated by BRENDA team
strain K12
UniProt
Manually annotated by BRENDA team
CHO fibroblasts
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain BY4741
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
2 forms of enzyme with some difference in primer preference
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Manually annotated by BRENDA team
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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
(A)15 + n ATP
(A)15+n + n diphosphate
show the reaction diagram
in the presence of ATP, the incorporation of several nucleotides into the RNA substrate is observed
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-
?
(A)n + ATP
(A)n+1 + diphosphate
show the reaction diagram
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-
-
?
(A)n + CTP
(A)n-C + diphosphate
show the reaction diagram
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-
-
?
(A)n + diphosphate
(A)n-1 + ATP
show the reaction diagram
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-
-
?
(A)n + GTP
(A)n-G + diphosphate
show the reaction diagram
-
-
-
?
2-aminopurine riboside triphosphate + RNA
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-O-(1-thiotriphosphate) + RNA
diphosphate + ?
show the reaction diagram
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SP-diastereomer
-
-
?
ATP + 3' untranslated region of mRNA
diphosphate + ?
show the reaction diagram
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-
-
?
ATP + adenosine(5')diphospho(5')adenosine
diphosphate + ?
show the reaction diagram
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i.e. AP2A
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-
?
ATP + adenosine(5')pentaphospho(5')adenosine
diphosphate + ?
show the reaction diagram
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i.e. AP5A
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-
?
ATP + adenosine(5')tetraphospho(5')adenosine
diphosphate + ?
show the reaction diagram
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i.e. AP4A
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-
?
ATP + adenosine(5')triphospho(5')adenosine
diphosphate + ?
show the reaction diagram
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i.e. AP3A
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-
?
ATP + AMP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + CMP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + CTP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + dGTP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + GDP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + GTP
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + guanosine
diphosphate + ?
show the reaction diagram
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-
-
-
?
ATP + guanosine(5')diphospho(5')guanosine
diphosphate + ?
show the reaction diagram
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i.e. GP2G
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-
?
ATP + guanosine(5')pentaphospho(5')guanosine
diphosphate + ?
show the reaction diagram
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i.e. GP5G
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-
?
ATP + guanosine(5')tetraphospho(5')guanosine
diphosphate + ?
show the reaction diagram
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i.e. GP4G
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-
?
ATP + guanosine(5')triphospho(5')guanosine
diphosphate + ?
show the reaction diagram
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i.e. GP3G
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?
ATP + IMP
diphosphate + ?
show the reaction diagram
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-
-
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?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
show the reaction diagram
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-
-
?
ATP + oligo(U)n
diphosphate + ?
show the reaction diagram
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?
ATP + RNA
?
show the reaction diagram
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
ATP + RNA primer
diphosphate + RNA primer-A
show the reaction diagram
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in absence of ATP: no activity with 8-Cl-ATP, and 8-amino-ATP results in chain termination, in presence of ATP: polyadenylation of the primer is blocked (inhibited) by 8-amino-ATP and 8-Cl-ATP
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?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
ATP + rRNA
diphosphate + ?
show the reaction diagram
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-
-
?
ATP + XTP
diphosphate + ?
show the reaction diagram
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-
-
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?
ATP + yeast tRNAiMet
diphosphate + ?
show the reaction diagram
in vitro-synthesized yeast tRNAiMet, but not the native tRNA is substrate
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?
CTP + RNA
diphosphate + ?
show the reaction diagram
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12% of the activity with ATP, adenylyltransferase A
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?
CTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
dATP + RNA
diphosphate + ?
show the reaction diagram
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15% of the activity with ATP
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?
mRNA of isoform gld-1 + ATP
polyadenylated mRNA of isoform gld-1 + diphosphate
show the reaction diagram
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reaction catalyzed by enzyme isoform GLD-2
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?
UTP + RNA
diphosphate + RNA(U)n
show the reaction diagram
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recombinant Cid1 shows a preference for UTP over ATP, the poly(U) polymerase activity of recombinant Cid1 out-competes its PAP activity under physiologically relevant conditions
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-aminopurine riboside triphosphate + RNA
?
show the reaction diagram
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-
-
?
ATP + RNA
?
show the reaction diagram
ATP + RNA
diphosphate + RNA(A)n
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NH4+
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maximal activity at 33 mM, inhibition above 150 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2'-dATP
3'-Acetyl-1'-benzyl-2'-methylpyrrolo[3,2-C]4-deoxyrifamycin
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3'-dATP
3-(4-Benzyl-2,6-dimethyl piperazinoiminomethyl)rifamycin SV
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3-(4-Ethylpiperazinoiminomethyl) rifamycin SV
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5-epi-sisomycin
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pH-dependent inhibition, non-competitive inhibitor for ATP
8-amino-ATP
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C-8 substitution influences sugar pucker conformation, which may affect yPAP efficiently
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8-aza-ATP
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slight inhibition
8-azido-ATP
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slight inhibition
8-bromo-ATP
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halogen modification at C-8 may negatively affect the ability of the enzyme to activate the ATP substrate or to transfer the AMP group from the enzyme to the RNA substrate
8-chloro-ATP
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adenosine 5'-(alpha,beta-methylenetriphosphate)
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adenylyl-(3'-5')adenosine
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Adenylyl-(3'-5')cytosine
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ADP
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inhibits hydrolytic reaction
alpha, beta-methylene-ATP
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a nonreactive ATP analogue
alpha-Amanitin
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AMP
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inhibits hydrolytic reaction
aurintricarboxylic acid
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Bentonite
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CaCl2
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remaining activity 3%
Calf thymus DNA
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CoCl2
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remaining activity 75%
cordycepin
Cordycepin 5'-triphosphate
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Cordycepin triphosphate
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5.0 mM
CuCl2
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remaining activity 0.1%
diphosphate
EDTA
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100% inhibition at 0.5 mM
GMP
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1 mM, complete inhibition of enzymic reaction with tRNA
heparin
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hygromycin B
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pH-dependent inhibition
Ionic strength
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kanamycin A
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pH-dependent inhibition
kanamycin B
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pH-dependent inhibition
KCl
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stimulation at low concentrations, at 300 mM, 15% inhibition, major poly(A) polymerase, 52% inhibition, minor poly(A) polymerase
lividomycin A
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pH-dependent inhibition
Mn2+
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high concentrations
N-ethylmaleimide
Na2HPO4
NaF
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10 mM, complete inhibition
neomycin B
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an increase in pH releases the neomycin B inhibitory effect on PAPgamma
Pancreatic ribonuclease
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paromomycin
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pH-dependent inhibition
PD98059
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induces partial inhibition of PAP phosphorylation at S537
phosphate
poly(C)
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Poly(dT)
Polyamines
Polyphosphate
Polyvinyl sulfate
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Proflavine
putrescine
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Ribonucleoside triphosphates other than ATP
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ribostamycin
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pH-dependent inhibition
rifampicin
rifamycin AF/013
Rifamycin B:N,N-diethylamide
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Rifamycin B:N,N-dipentylamide
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Rifamycin derivatives
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some derivatives are effective, others not
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rifamycin SV
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Rose bengal
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sisomicin
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pH-dependent inhibition, non-competitive inhibitor for ATP
small ubiquitin-like modifier
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in vitro sumoylation inhibits the activity of purified PAP
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Sodium vanadate
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spermidine
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spermine
tobramycin
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pH-dependent inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3',5'-AMP
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slight stimulation
Dinucleotide
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in presence of 0.5 mM ATP, activation in decreasing order: GP4G, GP3G, AP6A, GP2G, AP4A, AP2A, GP5G, AP5A, AP3A, activation at 0.01 mM is 4-10fold
dithiothreitol
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required
germ cell-specific gene 1 protein
TPAP interaction partner protein leading to redistribution of TPAP from the cytosol to the endoplasmic reticulum
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host factor I
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Hfq-PAP I interaction facilitates RNA recognition by PAP I
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KCl
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major poly(A) polymerase, optimal at 250 mM, minor poly(A) polymerase, optimal at 125 mM, inhibition of both above 250 mM
phosphatidylinositol 4,5-bisphosphate
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in the presence of 50 mM phosphatidylinositol 4,5-bisphosphate Star-PAP activity is markedly stimulated
Poly(U)
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stimulates
spermidine
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slight stimulation, 5 mM
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00092 - 0.00534
(A)15
0.0468 - 0.711
(A)n
0.0197
2-aminopurine riboside triphosphate
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0.028 - 2.191
ATP
0.1036 - 4.7
CTP
0.06
dATP
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30C, pH 8.5
0.055 - 0.062
GTP
0.01 - 0.3
oligo(A)
0.00039
oligo(A)12
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incubation 30 min at 30 C
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0.0005 - 0.037
oligo(A)14
0.0263
oligo(A)17C
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incubation at 30 C for 15 min in the presence of MgATP2-
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0.0468 - 0.0642
oligo(A)18
0.2
oligoadenylate
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in presence of Mg2+, pH 9.0, 35C
0.0036 - 0.36
Poly(A)
0.51 - 24.99
RNA (A)15
0.002
RNA primer
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0.007
short poly(A)
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additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.142 - 0.18
(A)15
0.002 - 30
ATP
0.43
CTP
Escherichia coli
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incubation 30 min at 30 C
3.33
Nucleotide
Zea mays
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0.0025 - 34.5
RNA(A)15
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.5 - 195.7
(A)15
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 1
3'-dATP
0.0019
8-amino-ATP
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incubation at 37 C for 20 min
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4 - 10
Poly(dT)
0.0002
polyphosphate P15
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competitive, 30C, pH 7.0
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0.0005
polyphosphate P4
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competitive, 30C, pH 7.0
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0939
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30C, pH 8.4
28.33
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35C, pH 9.0
3175
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37C, pH 8.3
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 8
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in presence of Mn2+
7
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Mn2+-activated enzyme
7.8 - 8.2
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8 - 8.5
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8.5
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polymerase I (chromatin)
9.5
-
adenylyltransferase A
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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pH 6: 47% (polymerase IIa) and 5% (polymerase IIb) of maximum activity, pH 9: 55% of maximum activity
7 - 8.5
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pH 7: about 40% of maximum activity, pH 8-8.5: maximum activity
7 - 8.8
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about 50% of maximum activity at pH 7.0 and pH 8.8
7.2 - 9.2
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pH 7.2: 55% of maximum activity, pH 9.2: 62% of maximum activity
7.5 - 9
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pH 7.5: 50% of maximum activity, pH 9.0: 15% of maximum activity
8 - 10
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pH 8: about 40% of maximum activity, pH 10: about 50% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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35
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assay at
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
primary foreskin fibroblasts
Manually annotated by BRENDA team
Q7XJ91, Q7XJ92, Q9LMT2
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Manually annotated by BRENDA team
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cryptobiotic gastrula
Manually annotated by BRENDA team
Q7XJ91, Q7XJ92, Q9LMT2
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Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
Coturnix sp.
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Manually annotated by BRENDA team
Q7XJ91, Q7XJ92, Q9LMT2
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Manually annotated by BRENDA team
Q7XJ91, Q7XJ92, Q9LMT2
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PAP I leader sequence directs the protein to the cellular membrane
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Manually annotated by BRENDA team
additional information
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plasmid
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Manually annotated by BRENDA team