EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.4.3 | Zn2+ | a zinc metalloenzyme | Bacillus subtilis |
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 | - |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.4.3 | Bacillus subtilis | - |
- |
- |
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 |
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 | - |
? |