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
ECTree
2.7.7.8 polyribonucleotide nucleotidyltransferaseAdvanced search results
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results (Molecular Weight
Molecular Weight on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase
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MOLECULAR WEIGHT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
100000
150000
200000
230000
240000
275000
48000
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alpha3,beta2 or alpha3,betan, x * 86000 + x * 48000, enzyme form B is obtained by keeping the ionic strength at 200 mM during purification on Sephadex G-200, at lower salt concentrations the beta subunit tends to dissociate and the enzyme reverts to the A form
580000 - 600000
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native and recombinant PNPase form a homo-multimer complex, gel filtration
71000
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x * 71000, enzyme form T, enzyme form I shows several bands of different molecular sizes, SDS-PAGE
80900
3 * 80900, about, sequence calculation, the trimeric hPNPase has a hexameric ring-like structure formed by six RNase PH domains, capped with a trimeric KH pore, the enzyme has a conserved GXXG motif in the KH domain, structural model of hPNPase, overview
86000
92000
additional information
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PNPase, the endoribonuclease RNase E, a DEAD-RNA helicase and the glycolytic enzyme enolase are associated with a high molecular weight complex, the degradosome
100000
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low molecular weight form catalyzing phosphorolysis but unable to catalyze the polymerization of NDP's, can only phosphorolyze short-chain polymers and requires higher Mg2+ ion concentration
100000
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2 * 100000, SDS-PAGE in the presence of 2-mercaptoethanol
200000
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this form requires Mn2+ for NDP polymerization and has a higher Km for poly(A) phosphorolysis
86000
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alpha3,beta2 or alpha3,betan, x * 86000 + x * 48000, enzyme form B is obtained by keeping the ionic strength at 200 mM during purification on Sephadex G-200, at lower salt concentrations the beta subunit tends to dissociate and the enzyme reverts to the A form
92000
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3 * 92000, SDS-PAGE, prior to purification the enzyme exists in oligomeric forms
