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
-
polyadenylation
-
phosphorolysis
-
degradosome
- helicase
-
exonuclease
-
exonucleolytic
-
stem-loop
- luteus
- micrococcus
- 5'-diphosphate
-
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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Metals Ions
Metals Ions on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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Ca2+
Cd2+
Co2+
Cu2+
K+
Mg2+
Mn2+
Na+
Ni2+
Zn2+
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no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme
Ca2+
-
no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme
Ca2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Co2+
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activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Cu2+
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activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Mg2+
-
maximal activation of ADP and GDP polymerization at 10 and 5 mM, respectively, inhibition at higher concentrations
Mg2+
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activity depends on divalent cation, order of efficiency: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Mg2+
substituting manganese for magnesium as the metal cofactor enables PNPase to nibble into the DNA tract. A 3'-phosphate group prevents RNA phosphorolysis when the metal cofactor is magnesium
Mg2+
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Mg2+ or Mn2+ required for activity, maximal activation at 1 mM Mg2+, inhibition above
Mg2+
-
optimal concentration for polymerization, phosphorolysis and ADP-phosphate exchange at 1 mM, 1-3 mM and 3 mM, respectively
Mg2+
-
divalent cation required, maximal activation at approx. 2 mM, Mg2+ is more effective than Mn2+ for polymerization, Mn2+ better activator in phosphorolytic reaction
Mg2+
-
optimal concentration for polymerization and phosphorolysis at 0.4 mM, optimum nucleotide/Mg2+ ratios for ADP, CDP and UDP are 4/1, 4/1 and 5/1, respectively
Mg2+
required, enzyme retains significant activity when the concentration is in the micromolar range
Mn2+
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in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA
Mn2+
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200000 Da form requires Mn2+ for NDP polymerization, polymerization of GDP proceedes efficiently in presence of Mn2+ at 60°C, polymerization with a mutant enzyme from E. coli Q13 requires Mn2+ rather than Mg2+
Mn2+
Mn2+ can substitute for Mg2+ as an essential co-factor for PNPase catalysis
Mn2+
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manganese can substitute for magnesium as the catalytic metal in PNPase, and RNA degradation
Mn2+
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activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Mn2+
with manganese as metal cofactor, PNPase can resect an RNA 3'-phosphate end, albeit 80fold slower than a 3'-OH
Mn2+
-
Mg2+ or Mn2+ required for activity, maximal activation at 0.06 mM Mn2+, inhibition above
Mn2+
-
optimal concentration for polymerization, phosphorolysis and ADP-phosphate exchange at 1 mM
Mn2+
-
divalent cation required, Mg2+ more effective than Mn2+ for polymerization, Mn2+ better activator in phosphorolytic reaction
Na+
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NaCl stimulates polymerization maximally at250 mM, inhibition above
Zn2+
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activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+