Information on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.8
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RECOMMENDED NAME
GeneOntology No.
polyribonucleotide nucleotidyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RNAn+1 + phosphate = RNAn + a nucleoside diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
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Pyrimidine metabolism
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SYSTEMATIC NAME
IUBMB Comments
polyribonucleotide:phosphate nucleotidyltransferase
ADP, IDP, GDP, UDP and CDP can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-12-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
KR. 170-4
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Manually annotated by BRENDA team
KR. 170-4
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
BaM-2
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-
Manually annotated by BRENDA team
strain BG214
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-
Manually annotated by BRENDA team
calf
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-
Manually annotated by BRENDA team
JM 98A
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
gene pnp
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-
Manually annotated by BRENDA team
gene pnp
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain JM83
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-
Manually annotated by BRENDA team
strain CA244
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-
Manually annotated by BRENDA team
Escherichia coli K-12 CA244
strain CA244
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Manually annotated by BRENDA team
gene pnp
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-
Manually annotated by BRENDA team
strain MG1693
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Manually annotated by BRENDA team
cock
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
MAC
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-
Manually annotated by BRENDA team
MAC
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-
Manually annotated by BRENDA team
strain KT2440, gene pnp
SwissProt
Manually annotated by BRENDA team
strain F-28
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
HB-8 strain
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Manually annotated by BRENDA team
wheat
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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
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
24-nucleotide RNA molecule + ADP
25-nucleotide RNA molecule + phosphate
show the reaction diagram
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when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
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r
24-nucleotide RNA molecule + phosphate
23-nucleotide RNA molecule + nucleoside diphosphate
show the reaction diagram
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when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
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r
microR-221 RNAn+1 + phosphate
microR-221 RNAn + ADP
show the reaction diagram
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recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184 as substrates, the recombinant enzyme selectively and preferentially degrades microRNA-221 in human melanoma cells
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r
microRNAn+1 + phosphate
microRNAn + ADP
show the reaction diagram
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recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184
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-
r
pJFD4 HpaI RNA+1 + phosphate
pJFD4 HpaI RNA + nucleoside diphosphate
show the reaction diagram
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derivative of SP82 phage RNA, arsenate can replace phosphate
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?
poly(A) + ADP
poly(A)+1 + phosphate
show the reaction diagram
poly(A)+1 + phosphate
poly(A) + ADP
show the reaction diagram
poly(C) + CDP
poly(C)+1 + phosphate
show the reaction diagram
poly(C)+1 + phosphate
poly(C) + ADP
show the reaction diagram
poly(G) + GDP
poly(G)+1 + phosphate
show the reaction diagram
poly(I) + IDP
poly(I)+1 + phosphate
show the reaction diagram
poly(U)+ UDP
poly(U)+1 + phosphate
show the reaction diagram
poly(U)+1 + phosphate
poly(U) + ADP
show the reaction diagram
rabbit globin mRNAn+1 + phosphate
ADP + rabbit globin mRNAn
show the reaction diagram
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only the poly(A) tail of the mRNA is removed
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?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
show the reaction diagram
RNA + ATP
RNA+1 + diphosphate
show the reaction diagram
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polymerization in the absence of phosphate
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r
RNA + CTP
RNA+1 + diphosphate
show the reaction diagram
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polymerization in the absence of phosphate
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r
RNA + GTP
RNA+1 + diphosphate
show the reaction diagram
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polymerization in the absence of phosphate
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r
RNA + UTP
RNA+1 + diphosphate
show the reaction diagram
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polymerization in the absence of phosphate
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r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + ADP
show the reaction diagram
yeast RNA+1 + phosphate
yeast RNA + nucleoside diphosphate
show the reaction diagram
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2% of activity with poly(U)
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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
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
show the reaction diagram
RNAn+1 + phosphate
RNAn + ADP
show the reaction diagram
G8TCS8
the enzyme catalyzes the processive phosphorolysis of RNA by using an inorganic phosphate to cleave the phosphodiester linkage at the 3'-end of a RNA chain
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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stimulates polymerization of ADP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Lithium salts
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activate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-Fluorouridine diphosphate
6-azauridine
Acridine orange
ADP
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inhibits ADP-phosphate exchange
beta,gamma-Imido-ATP
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5 mM, 28°C, presence of MgCl2, 50% residual activity
chlortetracycline
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competitive inhibition of ADP polymerization
citrate
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a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. PNPase-dependent cells show reduced growth in the presence of increased citrate concentration. In vitro, citrate directly binds and modulates PNPase activity, and the enzyme is inhibited by binding of metal-chelated citrate, predominantly complexed as magnesium-citrate, in the active site at physiological concentrations. In the contrary, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity
dATP
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5 mM, 28°C, presence of MgCl2, 39% residual activity
dGTP
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5 mM, 28°C, presence of MgCl2, 40% residual activity
GDP
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0.8 mM, more than 80% inhibition of ADP polymerization
GTP
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5 mM, 28°C, presence of MgCl2, 65% residual activity
hydrogen peroxide
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upon exposure of human cells, the amount of enzyme protein decreases rapidly
menadione
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upon exposure of human cells, the amount of enzyme protein decreases rapidly
Mg2+
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stimulates ADP polymerization maximally at 10 mM, GDP polymerization maximally at 5 mM, inhibition above
Na2HPO4
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0.0032 mM, complete inhibition
phosphate
phosphonic acid analog of ADP
Poly(A)
Poly(G)
rifamycin SV
Sucrose
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50%, approx. 50% inhibition of partially purified enzyme
synthetic polynucleotide
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additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP
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1.6 mM, 30% activation of ADP polymerization
Basic polypeptide
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peptide from Escherichia coli extract, enhances ADP-phosphate exchange
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Bis-(3-aminopropyl)-amine
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optimal polymerization activity requires presence, 2fold increase in activity at 30 mM
citrate
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a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome. PNPase-dependent cells show reduced growth in the presence of increased citrate concentration. In vitro, citrate directly binds and modulates PNPase activity, and the enzyme is inhibited by binding of metal-chelated citrate, predominantly complexed as magnesium-citrate, in the active site at physiological concentrations. In the contrary, metal-free citrate is bound at a vestigial active site, where it stimulates PNPase activity, this vestigial site as an allosteric binding pocket that recognizes metal-free citrate
cytidyldadenylate dinucleoside
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activates GDP polymerization
diphosphate
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activation of PNPase RNA synthesis activity at very low concentrations of phosphate
dithiothreitol
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similar activation as with 2-mercaptoethanol
interferon-beta
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close association between interferon-beta induced upregulation of enzyme and c-myc downregulation
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mercaptoethanol
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20 mM, 3fold activation
phosphate
poly-L-lysine
Polyarginine
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stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited
Polyornithine
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stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited
putrescine
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optimal polymerization activity requires polyamines, 2fold increase in activity at 30 mM
spermidine
spermine
additional information