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Literature summary extracted from

  • Ochoa, S.; Mii, S.
    Enzymatic synthesis of polynucleotides. IV. Purification and properties of polynucleotide phosphorylase of Azobacter vinelandii (1961), J. Biol. Chem., 236, 3303-3311.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.8 Azotobacter vinelandii
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.8 ammonium sulfate, ethanol, calcium phosphate gel, protamine, hydroxylapatite Azotobacter vinelandii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.8 39.6
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Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.8 poly(G) + GDP much lower activity than with ADP, activity depends on polyribonucleotide primer Azotobacter vinelandii poly(G)+1 + phosphate
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?
2.7.7.8 ribonucleoside 5'-diphosphate + phosphate
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Azotobacter vinelandii ribonucleoside 5'-diphosphate + phosphate exchange reaction ?
2.7.7.8 RNAn + a nucleoside diphosphate synthesis of poly(A): no primer addition required if large amounts of enzyme or Mg2+ are used, with small amounts of either component a primer is required, poly(G) synthesis: primer required Azotobacter vinelandii RNAn+1 + phosphate
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?