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Literature summary extracted from

  • Yao, L.; Cukier, R.I.; Yan, H.
    Catalytic mechanism of guanine deaminase: an ONIOM and molecular dynamics study (2007), J. Phys. Chem. B, 111, 4200-4210.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.3 Zn2+ a zinc metalloenzyme Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.3 guanine + H2O Bacillus subtilis
-
 xanthine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.3 Bacillus subtilis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.4.3 guanine + H2O = xanthine + NH3 catalytic mechanism, quantum mechanical calculations using multilayered ONIOM and molecular dynamics study, the active-site residues of the enzyme do not affect the tautomeric state of guanine, Glu55 and Asp114 play important roles in proton shuttling in the reaction, proton transfer from a Zn-bound water to protonate Asp114, which can then transfer its proton to the N3 of the bound guanine, facilitating the nucleophilic attack on C2 of the guanine by the Zn-bound hydroxide to form a tetrahedral intermediate. Glu55 then transfers a proton from the Zn-hydroxide to the amino group of the reaction intermediate, ammonia leaves the active site, and xanthine is freed by the cleavage of the Zn-O2 bond Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.3 guanine + H2O
-
 Bacillus subtilis xanthine + NH3
-
 ?
3.5.4.3 guanine + H2O substrate binding structure and tautomerization of the bound guanine, reaction steps in a detailed overview Bacillus subtilis xanthine + NH3
-
 ?