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Literature summary for 3.1.30.2 extracted from

  • Pires de Castro, C.S.; Rodrigues SouzaDe, J.; Bloch, C.
    Mechanism of DNA cleavage catalyzed by mung bean nuclease (2004), Inorg. Chim. Acta, 357, 2579-2592.
No PubMed abstract available
Search for more literature for 3.1.30.2

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the enzyme is a zinc metalloprotein, three zinc ions interact with the DNA substrate and have different roles in catalysis, e.g. stabilization of the transition state and as reaction nucleophile, binding structures and kinetics, overview Vigna radiata

Organism

Organism UniProt Comment Textmining
Vigna radiata
-
 i.e. Phaseolus radiatus
-

Reaction

Reaction Comment Organism Reaction ID
endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products DNA cleavage stereochemistry and mechanism involving interaction of DNA with three zinc ions, the enzyme contains a cocatalytic zinc site Vigna radiata
a

Source Tissue

Source Tissue Comment Organism Textmining
seed mung bean Vigna radiata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ds-oligoDNA + H2O
-
 Vigna radiata ?
-
 ?
lambda phage DNA + H2O
-
 Vigna radiata ?
-
 ?
ss-oligoDNA + H2O
-
 Vigna radiata ?
-
 ?

Synonyms

Synonyms Comment Organism
mung bean nuclease
-
 Vigna radiata