2.7.7.8: polyribonucleotide nucleotidyltransferase
This is an abbreviated version!
For detailed information about polyribonucleotide nucleotidyltransferase, go to the full flat file.
Word Map on EC 2.7.7.8
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2.7.7.8
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rnase
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exoribonuclease
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polya
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ribonuclease
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polymerization
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polyadenylation
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phosphorolysis
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degradosome
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helicase
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exonuclease
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exonucleolytic
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stem-loop
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luteus
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micrococcus
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5'-diphosphate
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rna-binding
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kh
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hfq
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oligoribonucleotides
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rna-degrading
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heteropolymeric
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antibioticus
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dead-box
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lysodeikticus
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primer-independent
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synthesis
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molecular biology
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medicine
- 2.7.7.8
- rnase
- exoribonuclease
- polya
- ribonuclease
- polymerization
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polyadenylation
-
phosphorolysis
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degradosome
- helicase
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exonuclease
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exonucleolytic
-
stem-loop
- luteus
- micrococcus
- 5'-diphosphate
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rna-binding
- kh
- hfq
- oligoribonucleotides
-
rna-degrading
-
heteropolymeric
- antibioticus
-
dead-box
- lysodeikticus
-
primer-independent
- synthesis
- molecular biology
- medicine
Reaction
Synonyms
AtcpPNPase, AtmtPNPase, chloroplast PNPase, cpPNPase, hPNPase(old-35), hPNPaseold-35, nucleoside diphosphate:polynucleotidyl transferase, nucleotidyltransferase, polyribonucleotide, PNP, PNPase, PNPT1, polynucleotide phosphorylase, polyribonucleotide phosphorylase, RNase PH
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Activating Compound
Activating Compound on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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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
diphosphate
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activation of PNPase RNA synthesis activity at very low concentrations of phosphate
interferon-beta
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close association between interferon-beta induced upregulation of enzyme and c-myc downregulation
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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
KCl
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salt is absolutely required for activity, maximal activity between 250 mM, inhibition above 1M
NaCl
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salt is absolutely required for activity, maximal activity at 250 mM, inhibition above 1 M
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400 mM, 3 and 7fold activation of ADP polymerization and poly(A) phosphorolysis, respectively
phosphate
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degradation activity of chloroplast PNPase is dramatically enhanced, polymerization activity in the absence of phosphate
phosphate
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maximal activation of recombinant PNPase RNA-derading activity at 20 mM
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stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited
poly-L-lysine
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0.25 mg/ml, 78fold activation in the presence of 10 mM NaCl, 5fold activation in the presence of 250 mM NaCl
spermidine
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optimal polymerization activity requires polyamines, 1.4fold increase in activity at 30 mM
spermine
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optimal polymerization activity requires polyamines, 2fold increase in activity at 30 mM
the enzyme expression is induced upon cold shock, transcriptional regulation, overview
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additional information
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the enzyme expression is induced upon cold shock, transcriptional regulation, overview
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