Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | residues His62, Cys91, and Cys94 are very important in coordinating the zinc cation | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q12178 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | Q12178 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cytosine + H2O | - |
Saccharomyces cerevisiae | uracil + NH3 | - |
? | |
cytosine + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | uracil + NH3 | - |
? | |
additional information | the rate-determining step of the reaction concerns the breaking of the product-metal binding state and has a barrier of about 18 kcal/mol. The protonation of cytosine by Glu64 in the substrate binding stage as well as the product transport step are also important and influence the whole catalytic efficiency, due to their considerable barriers (12-13 kcal/mol). The driving force for the overall enzymatic reaction likely comes from the reactant delivery to the active site of the protein | Saccharomyces cerevisiae | ? | - |
? | |
additional information | the rate-determining step of the reaction concerns the breaking of the product-metal binding state and has a barrier of about 18 kcal/mol. The protonation of cytosine by Glu64 in the substrate binding stage as well as the product transport step are also important and influence the whole catalytic efficiency, due to their considerable barriers (12-13 kcal/mol). The driving force for the overall enzymatic reaction likely comes from the reactant delivery to the active site of the protein | Saccharomyces cerevisiae ATCC 204508 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FCY1 | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | residues His62, Cys91, and Cys94 are very important in coordinating the zinc cation. The bound water molecule and Glu64 are crucial in the formation of the reactant-metal binding state, the subsequent chemical reaction, and the cleavage of the product-metal binding state. Asn51, Glu64, and Asp155 form hydrogen bonds with the product and block the product from moving away from the protein. Phe114 and Trp152 play a dual role of gating and guiding in the pocket of exit | Saccharomyces cerevisiae |