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Literature summary for 4.6.1.21 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
Search for more literature for 4.6.1.21

Activating Compound

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

Application Comment Organism
analysis
-
 Enterobacter sp.

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Enterobacter sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Enterobacter sp.

Storage Stability

Storage Stability Organism
-20°C Enterobacter sp.

Substrates and Products (Substrate)

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