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Literature summary for 3.5.4.1 extracted from

  • Zhao, Y.; She, N.; Zhang, X.; Wang, C.; Mo, Y.
    Product release mechanism and the complete enzyme catalysis cycle in yeast cytosine deaminase (yCD) A computational study (2017), Biochim. Biophys. Acta, 1865, 1020-1029 .
    View publication on PubMed
Search for more literature for 3.5.4.1

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ residues His62, Cys91, and Cys94 are very important in coordinating the zinc cation Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q12178
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Saccharomyces cerevisiae ATCC 204508 Q12178
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cytosine + H2O
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 Saccharomyces cerevisiae uracil + NH3
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 ?
cytosine + H2O
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 Saccharomyces cerevisiae ATCC 204508 uracil + NH3
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 ?
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

Synonyms Comment Organism
FCY1
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 Saccharomyces cerevisiae

General Information

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