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Literature summary for 3.5.4.1 extracted from

  • Xu, Q.; Guo, H.; Gorin, A.; Guo, H.
    Stabilization of a transition-state analogue at the active site of yeast cytosine deaminase: importance of proton transfers (2007), J. Phys. Chem. B, 111, 6501-6506.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
PDB ID 1UAQ, structure analysis and comparison to the quantum mechanical/molecular mechanical molecular dynamics simulation model, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cytosine + H2O Saccharomyces cerevisiae
-
uracil + NH3
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q12178
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cytosine + H2O
-
Saccharomyces cerevisiae uracil + NH3
-
?
pyrimidin-2-one + H2O stabilization of a transition-state analogue at the active site of cytosine deaminase with importance of proton transfer from the Zn hydroxide group to Glu64 during the nucleophilic attack, quantum mechanical/molecular mechanical molecular dynamics and free energy simulations, active site structure, overview Saccharomyces cerevisiae (4R)-hydroxyl-3,4-dihydropyrimidine + ?
-
?