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Literature summary extracted from

  • Frank, J.J.; Hawk, I.A.; Levy, C.C.
    Peptides isolated from Enterobacter nuclease as potential polyamine binding sites (1976), Biochim. Biophys. Acta, 432, 369-380.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.21 putrescine enhances activity against poly(C) and yeast RNA Enterobacter sp.
4.6.1.21 spermidine enhances activity against poly(C) and yeast RNA, reverses inhibition by poly(G) by removal of inhibitor from the enzymes surface Enterobacter sp.
4.6.1.21 spermine enhances activity against poly(C) and yeast RNA, reverses inhibition by poly(G) by removal of inhibitor from the enzymes surface Enterobacter sp.

Application

EC Number Application Comment Organism
4.6.1.21 analysis
-
Enterobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.21 Poly(A)
-
Enterobacter sp.
4.6.1.21 Poly(G) inhibition at a concentration of 0.25 nM is complete Enterobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.21 Ca2+ stimulating Enterobacter sp.
4.6.1.21 Mg2+ stimulating Enterobacter sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.6.1.21 RNA + H2O Enterobacter sp. preferential cleavage at CpA nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
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Organism

EC Number Organism UniProt Comment Textmining
4.6.1.21 Enterobacter sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.21
-
Enterobacter sp.

Storage Stability

EC Number Storage Stability Organism
4.6.1.21 -20°C Enterobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.6.1.21 RNA + H2O preferential cleavage at CpA Enterobacter sp. nucleoside 3'-phosphates and 3'-phosphooligonucleotides and 2',3'-cyclic phosphates
-
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