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Literature summary extracted from

  • Littauer, U.Z.; Soreq, H.
    Polynucleotide phosphorylase (1982), The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. ), 15B, 517-553.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.8 Basic polypeptide peptide from Escherichia coli extract, enhances ADP-phosphate exchange Geobacillus stearothermophilus
2.7.7.8 poly-L-lysine stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited Clostridium perfringens
2.7.7.8 Polyarginine stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited Clostridium perfringens
2.7.7.8 Polyornithine stimulation of poly(A) synthesis, phosphorolysis of poly(A) is inhibited Clostridium perfringens
2.7.7.8 spermidine
-
 Nicotiana tabacum
2.7.7.8 spermidine 0.1-1.0 mM, activates ADP-phosphate exchange 2fold Escherichia coli
2.7.7.8 spermine
-
 Nicotiana tabacum
2.7.7.8 spermine 0.1-1.0 mM, activates ADP-phosphate exchange 2fold Escherichia coli

General Stability

EC Number General Stability Organism
2.7.7.8 highly susceptible to proteolysis Clostridium perfringens
2.7.7.8 sensitive to proteolytic digestion Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 sensitive to proteolytic digestion Cavia porcellus
2.7.7.8 sensitive to proteolytic digestion Thermus aquaticus
2.7.7.8 sensitive to proteolytic digestion Sinorhizobium meliloti
2.7.7.8 sensitive to proteolytic digestion Escherichia coli
2.7.7.8 sensitive to proteolytic digestion Rattus norvegicus
2.7.7.8 sensitive to proteolytic digestion Geobacillus stearothermophilus
2.7.7.8 sensitive to proteolytic digestion Nicotiana tabacum
2.7.7.8 sensitive to proteolytic digestion Halobacterium salinarum
2.7.7.8 sensitive to proteolytic digestion Enterococcus faecalis
2.7.7.8 sensitive to proteolytic digestion Streptococcus pyogenes
2.7.7.8 sensitive to proteolytic digestion Achromobacter sp.
2.7.7.8 sensitive to proteolytic digestion Micrococcus luteus
2.7.7.8 sensitive to proteolytic digestion Azotobacter vinelandii
2.7.7.8 sensitive to proteolytic digestion Rhodospirillum rubrum
2.7.7.8 sensitive to proteolytic digestion Brevibacterium sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.8 5-Fluorouridine diphosphate
-
 Achromobacter sp.
2.7.7.8 5-Fluorouridine diphosphate
-
 Azotobacter vinelandii
2.7.7.8 5-Fluorouridine diphosphate
-
 Brevibacterium sp.
2.7.7.8 5-Fluorouridine diphosphate
-
 Cavia porcellus
2.7.7.8 5-Fluorouridine diphosphate
-
 Enterococcus faecalis
2.7.7.8 5-Fluorouridine diphosphate
-
 Escherichia coli
2.7.7.8 5-Fluorouridine diphosphate
-
 Geobacillus stearothermophilus
2.7.7.8 5-Fluorouridine diphosphate
-
 Halobacterium salinarum
2.7.7.8 5-Fluorouridine diphosphate
-
 Micrococcus luteus
2.7.7.8 5-Fluorouridine diphosphate
-
 Nicotiana tabacum
2.7.7.8 5-Fluorouridine diphosphate
-
 Rattus norvegicus
2.7.7.8 5-Fluorouridine diphosphate
-
 Rhodospirillum rubrum
2.7.7.8 5-Fluorouridine diphosphate
-
 Sinorhizobium meliloti
2.7.7.8 5-Fluorouridine diphosphate
-
 Streptococcus pyogenes
2.7.7.8 5-Fluorouridine diphosphate
-
 Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 5-Fluorouridine diphosphate
-
 Thermus aquaticus
2.7.7.8 6-azauridine
-
 Achromobacter sp.
2.7.7.8 6-azauridine
-
 Azotobacter vinelandii
2.7.7.8 6-azauridine
-
 Brevibacterium sp.
2.7.7.8 6-azauridine
-
 Cavia porcellus
2.7.7.8 6-azauridine
-
 Enterococcus faecalis
2.7.7.8 6-azauridine
-
 Escherichia coli
2.7.7.8 6-azauridine
-
 Geobacillus stearothermophilus
2.7.7.8 6-azauridine
-
 Halobacterium salinarum
2.7.7.8 6-azauridine
-
 Micrococcus luteus
2.7.7.8 6-azauridine
-
 Nicotiana tabacum
2.7.7.8 6-azauridine
-
 Rattus norvegicus
2.7.7.8 6-azauridine
-
 Rhodospirillum rubrum
2.7.7.8 6-azauridine
-
 Sinorhizobium meliloti
2.7.7.8 6-azauridine
-
 Streptococcus pyogenes
2.7.7.8 6-azauridine
-
 Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 6-azauridine
-
 Thermus aquaticus
2.7.7.8 Acridine orange
-
 Achromobacter sp.
2.7.7.8 Acridine orange
-
 Azotobacter vinelandii
2.7.7.8 Acridine orange
-
 Brevibacterium sp.
2.7.7.8 Acridine orange
-
 Cavia porcellus
2.7.7.8 Acridine orange
-
 Enterococcus faecalis
2.7.7.8 Acridine orange
-
 Escherichia coli
2.7.7.8 Acridine orange
-
 Geobacillus stearothermophilus
2.7.7.8 Acridine orange
-
 Halobacterium salinarum
2.7.7.8 Acridine orange
-
 Micrococcus luteus
2.7.7.8 Acridine orange
-
 Nicotiana tabacum
2.7.7.8 Acridine orange
-
 Rattus norvegicus
2.7.7.8 Acridine orange
-
 Rhodospirillum rubrum
2.7.7.8 Acridine orange
-
 Sinorhizobium meliloti
2.7.7.8 Acridine orange
-
 Streptococcus pyogenes
2.7.7.8 Acridine orange
-
 Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Acridine orange
-
 Thermus aquaticus
2.7.7.8 heparin
-
 Bacillus amyloliquefaciens
2.7.7.8 phosphonic acid analog of ADP
-
 Achromobacter sp.
2.7.7.8 phosphonic acid analog of ADP
-
 Azotobacter vinelandii
2.7.7.8 phosphonic acid analog of ADP
-
 Brevibacterium sp.
2.7.7.8 phosphonic acid analog of ADP
-
 Cavia porcellus
2.7.7.8 phosphonic acid analog of ADP
-
 Enterococcus faecalis
2.7.7.8 phosphonic acid analog of ADP
-
 Escherichia coli
2.7.7.8 phosphonic acid analog of ADP
-
 Geobacillus stearothermophilus
2.7.7.8 phosphonic acid analog of ADP
-
 Halobacterium salinarum
2.7.7.8 phosphonic acid analog of ADP
-
 Micrococcus luteus
2.7.7.8 phosphonic acid analog of ADP
-
 Nicotiana tabacum
2.7.7.8 phosphonic acid analog of ADP
-
 Rattus norvegicus
2.7.7.8 phosphonic acid analog of ADP
-
 Rhodospirillum rubrum
2.7.7.8 phosphonic acid analog of ADP
-
 Sinorhizobium meliloti
2.7.7.8 phosphonic acid analog of ADP
-
 Streptococcus pyogenes
2.7.7.8 phosphonic acid analog of ADP
-
 Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 phosphonic acid analog of ADP
-
 Thermus aquaticus
2.7.7.8 rifamycin SV
-
 Bacillus amyloliquefaciens
2.7.7.8 synthetic polynucleotide
-
 Bacillus amyloliquefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.8 0.05
-
 Mg2+
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.8 cell membrane
-
 Halobacterium salinarum
-
-
2.7.7.8 cell membrane
-
 Enterococcus faecalis
-
-
2.7.7.8 cell membrane
-
 Streptococcus pyogenes
-
-
2.7.7.8 endoplasmic reticulum
-
 Rattus norvegicus 5783
-
2.7.7.8 membrane membrane vesicles Escherichia coli 16020
-
2.7.7.8 mitochondrion
-
 Cavia porcellus 5739
-
2.7.7.8 mitochondrion
-
 Rattus norvegicus 5739
-
2.7.7.8 soluble
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.8 Ca2+ no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme Escherichia coli
2.7.7.8 Ca2+ no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme Geobacillus stearothermophilus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Cd2+ can partially replace Mg2+ in activation Brevibacterium sp.
2.7.7.8 Co2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Co2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Co2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Co2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Co2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Co2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Co2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Co2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Co2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Co2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Co2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Co2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Co2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Co2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Co2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Co2+ can partially replace Mg2+ in activation Brevibacterium sp.
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Cu2+ can partially replace Mg2+ in activation Brevibacterium sp.
2.7.7.8 K+
-
 Nicotiana tabacum
2.7.7.8 K+ potassium salts activate Micrococcus luteus
2.7.7.8 K+ activates polymerization Micrococcus luteus
2.7.7.8 Lithium salts activate Micrococcus luteus
2.7.7.8 Mg2+ required for activity Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Mg2+ required for activity Cavia porcellus
2.7.7.8 Mg2+ required for activity Thermus aquaticus
2.7.7.8 Mg2+ required for activity Sinorhizobium meliloti
2.7.7.8 Mg2+ required for activity Escherichia coli
2.7.7.8 Mg2+ required for activity Rattus norvegicus
2.7.7.8 Mg2+ required for activity Geobacillus stearothermophilus
2.7.7.8 Mg2+ required for activity Nicotiana tabacum
2.7.7.8 Mg2+ required for activity Halobacterium salinarum
2.7.7.8 Mg2+ required for activity Enterococcus faecalis
2.7.7.8 Mg2+ required for activity Streptococcus pyogenes
2.7.7.8 Mg2+ required for activity Achromobacter sp.
2.7.7.8 Mg2+ required for activity Micrococcus luteus
2.7.7.8 Mg2+ required for activity Azotobacter vinelandii
2.7.7.8 Mg2+ required for activity Bacillus amyloliquefaciens
2.7.7.8 Mg2+ required for activity Rhodospirillum rubrum
2.7.7.8 Mg2+ required for activity Brevibacterium sp.
2.7.7.8 Mg2+ Km: 0.05 mM Escherichia coli
2.7.7.8 Mg2+ 100000 Da form requires high Mg2+ concentrations Escherichia coli
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Bacillus amyloliquefaciens
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Mn2+ can partially replace Mg2+ in activation Brevibacterium sp.
2.7.7.8 Mn2+ 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+ Escherichia coli
2.7.7.8 Mn2+ stimulates polymerization more efficiently than Mg2+ Achromobacter sp.
2.7.7.8 Na+ activates polymerization Micrococcus luteus
2.7.7.8 Na+ sodium salts activate Micrococcus luteus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Ni2+ can partially replace Mg2+ in activation Brevibacterium sp.
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Cavia porcellus
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Thermus aquaticus
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Sinorhizobium meliloti
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Escherichia coli
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Rattus norvegicus
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Geobacillus stearothermophilus
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Nicotiana tabacum
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Halobacterium salinarum
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Enterococcus faecalis
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Streptococcus pyogenes
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Achromobacter sp.
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Micrococcus luteus
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Azotobacter vinelandii
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Rhodospirillum rubrum
2.7.7.8 Zn2+ can partially replace Mg2+ in activation Brevibacterium sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.8 48000
-
 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 Escherichia coli
2.7.7.8 51000
-
 4 * 51000 Geobacillus stearothermophilus
2.7.7.8 76000
-
 2 * 76000, SDS-PAGE Rhodospirillum rubrum
2.7.7.8 86000
-
 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 Escherichia coli
2.7.7.8 100000
-
 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 Escherichia coli
2.7.7.8 160000
-
 gel filtration Rhodospirillum rubrum
2.7.7.8 200000
-
-
 Azotobacter vinelandii
2.7.7.8 200000
-
 this form requires Mn2+ for NDP polymerization and has a higher Km for poly(A) phosphorolysis Escherichia coli
2.7.7.8 237000
-
 sedimentation equilibrium Micrococcus luteus
2.7.7.8 252000
-
 enzyme form A Escherichia coli
2.7.7.8 365000
-
 enzyme form B Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.8 Achromobacter sp.
-
 KR. 170-4
-
2.7.7.8 Achromobacter sp. KR. 170-4
-
 KR. 170-4
-
2.7.7.8 Azotobacter vinelandii
-
-
-
2.7.7.8 Bacillus amyloliquefaciens
-
 BaM-2
-
2.7.7.8 Bacillus amyloliquefaciens BaM-2
-
 BaM-2
-
2.7.7.8 Brevibacterium sp.
-
-
-
2.7.7.8 Cavia porcellus
-
-
-
2.7.7.8 Clostridium perfringens
-
-
-
2.7.7.8 Enterococcus faecalis
-
-
-
2.7.7.8 Escherichia coli
-
-
-
2.7.7.8 Geobacillus stearothermophilus
-
-
-
2.7.7.8 Halobacterium salinarum
-
-
-
2.7.7.8 Micrococcus luteus
-
-
-
2.7.7.8 Nicotiana tabacum
-
 tobacco mosaic virus-infected
-
2.7.7.8 Rattus norvegicus
-
-
-
2.7.7.8 Rhodospirillum rubrum
-
-
-
2.7.7.8 Sinorhizobium meliloti
-
-
-
2.7.7.8 Streptococcus pyogenes
-
-
-
2.7.7.8 Synechococcus elongatus PCC 7942 = FACHB-805
-
-
-
2.7.7.8 Thermus aquaticus
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.7.8 after heating at 100°C for 1 min 25-30% of the original activity can be recovered by dissolving the precipitate in 6 M guanidine-HCl followed by dialysis Escherichia coli

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.8 leaf
-
 Nicotiana tabacum
-
2.7.7.8 liver
-
 Cavia porcellus
-
2.7.7.8 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.8 poly(A) + ADP
-
 Synechococcus elongatus PCC 7942 = FACHB-805 poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Cavia porcellus poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Thermus aquaticus poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Sinorhizobium meliloti poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Escherichia coli poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Geobacillus stearothermophilus poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Nicotiana tabacum poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Halobacterium salinarum poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Enterococcus faecalis poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Streptococcus pyogenes poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Achromobacter sp. poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Micrococcus luteus poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Azotobacter vinelandii poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Bacillus amyloliquefaciens poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Rhodospirillum rubrum poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Brevibacterium sp. poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(A) + ADP
-
 Bacillus amyloliquefaciens BaM-2 poly(A)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Synechococcus elongatus PCC 7942 = FACHB-805 poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Cavia porcellus poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Thermus aquaticus poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Sinorhizobium meliloti poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Escherichia coli poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Geobacillus stearothermophilus poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Nicotiana tabacum poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Halobacterium salinarum poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Enterococcus faecalis poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Streptococcus pyogenes poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Achromobacter sp. poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Micrococcus luteus poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Azotobacter vinelandii poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Rhodospirillum rubrum poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(C) + CDP
-
 Brevibacterium sp. poly(C)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Synechococcus elongatus PCC 7942 = FACHB-805 poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Cavia porcellus poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Thermus aquaticus poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Sinorhizobium meliloti poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Escherichia coli poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Geobacillus stearothermophilus poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Nicotiana tabacum poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Halobacterium salinarum poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Enterococcus faecalis poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Streptococcus pyogenes poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Achromobacter sp. poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Micrococcus luteus poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Azotobacter vinelandii poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Bacillus amyloliquefaciens poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Rhodospirillum rubrum poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Brevibacterium sp. poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(G) + GDP
-
 Bacillus amyloliquefaciens BaM-2 poly(G)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Synechococcus elongatus PCC 7942 = FACHB-805 poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Cavia porcellus poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Thermus aquaticus poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Sinorhizobium meliloti poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Escherichia coli poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Geobacillus stearothermophilus poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Nicotiana tabacum poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Halobacterium salinarum poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Enterococcus faecalis poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Streptococcus pyogenes poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Achromobacter sp. poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Micrococcus luteus poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Azotobacter vinelandii poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Rhodospirillum rubrum poly(I)+1 + phosphate
-
 r
2.7.7.8 poly(I) + IDP
-
 Brevibacterium sp. poly(I)+1 + phosphate
-
 r
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Synechococcus elongatus PCC 7942 = FACHB-805 ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Cavia porcellus ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Thermus aquaticus ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Sinorhizobium meliloti ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Escherichia coli ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Rattus norvegicus ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Geobacillus stearothermophilus ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Nicotiana tabacum ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Halobacterium salinarum ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Enterococcus faecalis ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Streptococcus pyogenes ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Achromobacter sp. ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Micrococcus luteus ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Azotobacter vinelandii ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Bacillus amyloliquefaciens ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Rhodospirillum rubrum ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Brevibacterium sp. ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
-
 Bacillus amyloliquefaciens BaM-2 ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Rattus norvegicus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Rattus norvegicus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Rattus norvegicus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Bacillus amyloliquefaciens RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Rattus norvegicus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Bacillus amyloliquefaciens RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Synechococcus elongatus PCC 7942 = FACHB-805 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Cavia porcellus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Thermus aquaticus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Sinorhizobium meliloti RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Escherichia coli RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Rattus norvegicus RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Geobacillus stearothermophilus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Nicotiana tabacum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Halobacterium salinarum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Enterococcus faecalis RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Streptococcus pyogenes RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Achromobacter sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Micrococcus luteus RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Azotobacter vinelandii RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Rhodospirillum rubrum RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds Brevibacterium sp. RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Bacillus amyloliquefaciens BaM-2 RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Bacillus amyloliquefaciens BaM-2 RNAn+1 + phosphate
-
 ?
2.7.7.8 RNAn + a nucleoside diphosphate specificity overview Achromobacter sp. KR. 170-4 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of IDP Achromobacter sp. KR. 170-4 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of CDP Achromobacter sp. KR. 170-4 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of GDP Achromobacter sp. KR. 170-4 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn + a nucleoside diphosphate polymerization of ADP Achromobacter sp. KR. 170-4 RNAn+1 + phosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Synechococcus elongatus PCC 7942 = FACHB-805 RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Cavia porcellus RNAn + a nucleoside diphosphate
-
 ir
2.7.7.8 RNAn+1 + phosphate
-
 Thermus aquaticus RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Sinorhizobium meliloti RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Escherichia coli RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Rattus norvegicus RNAn + a nucleoside diphosphate
-
 ir
2.7.7.8 RNAn+1 + phosphate
-
 Geobacillus stearothermophilus RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Nicotiana tabacum RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Halobacterium salinarum RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Enterococcus faecalis RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Streptococcus pyogenes RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Achromobacter sp. RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Micrococcus luteus RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Azotobacter vinelandii RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Rhodospirillum rubrum RNAn + a nucleoside diphosphate
-
 r
2.7.7.8 RNAn+1 + phosphate
-
 Brevibacterium sp. RNAn + a nucleoside diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.8 ?
-
 Micrococcus luteus
2.7.7.8 ? 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 Escherichia coli
2.7.7.8 dimer 2 * 76000, SDS-PAGE Rhodospirillum rubrum
2.7.7.8 tetramer
-
 Thermus aquaticus
2.7.7.8 tetramer 4 * 51000 Geobacillus stearothermophilus
2.7.7.8 trimer
-
 Micrococcus luteus
2.7.7.8 trimer alpha3, 3 * 84000-95000, enzyme form A, ultrastructural observations Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Synechococcus elongatus PCC 7942 = FACHB-805
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Cavia porcellus
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Thermus aquaticus
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Sinorhizobium meliloti
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Escherichia coli
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Rattus norvegicus
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Geobacillus stearothermophilus
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Nicotiana tabacum
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Halobacterium salinarum
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Enterococcus faecalis
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Streptococcus pyogenes
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Achromobacter sp.
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Micrococcus luteus
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Azotobacter vinelandii
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Rhodospirillum rubrum
2.7.7.8 additional information
-
 stabilized against heat inactivation by the presence of NDP's but not by NMP's, NTP's, DNA or substrate oligonucleotides with free 3'-OH termini Brevibacterium sp.
2.7.7.8 55
-
 unstable above Escherichia coli
2.7.7.8 65
-
-
 Thermus aquaticus
2.7.7.8 65
-
 rapid and irreversible inactivation Escherichia coli