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Literature summary extracted from

  • Stevens, A.; Hilmoe, R.J.
    Studies on a nuclease from Azotobacter agilis. II. Hydrolysis of ribonucleic and deoxyribonucleic acids (1960), J. Biol. Chem., 235, 3023-3027.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.30.2 Urea 2 M, stimulation Azotobacter agilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.30.2 Mg2+ increases hydrolysis rate of EDTA-dialyzed RNA, no effect on hydrolysis of undialyzed RNA, inhibition at high concentrations Azotobacter agilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.30.2 Mg2+ increases hydrolysis rate of EDTA-dialyzed RNA, no effect on hydrolysis of undialyzed RNA, inhibition at high concentrations Azotobacter agilis

Organism

EC Number Organism UniProt Comment Textmining
3.1.30.2 Azotobacter agilis
-
similar enzyme
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.30.2 DNA + H2O
-
Azotobacter agilis 5'-phosphonucleotides + 5'-phosphomononucleotides
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.30.2 More similar enzymes: silkworm nuclease, potato nuclease, Azotobacter nuclease Azotobacter agilis
3.1.30.2 More mung bean nuclease has specificity for single-stranded substrates, see E.C. 3.1.30.1 Azotobacter agilis