3.7.1.8	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate	although MCP hydrolases have a catalytic serine in the active site, the mechanism proceeds via a geminal diol, rather than an acyl-enzyme intermediate, reaction mechanism of the hydrolysis reaction, overview. MCP hydrolases accept alternative nucleophiles in addition to water, and accepts hydroxylamine in the C-C cleavage reaction. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview	-, 733047	
3.7.1.8	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate	catalytic mechanism involving enol-to-keto tautomerization that consists of two elementary reactions, the calculated Boltzmann weighted average barriers favor a substrate-assisted acylation mechanism, and the most feasible acylation pathway involves a catalytic triad, Ser-His-Asp. The product (2-hydroxypenta-2,4-dienoic acid) of the acylation process is replaced by three water molecules, and one of which is involved in the deacylation process, quantum mechanics/molecular mechanics study, overview	735243	
3.7.1.8	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate	formation of a catalytic intermediate carbanion during hydrolysis, the carbanion abstracts a proton from Ser112, thereby completing tautomerization and generating a serinate for nucleophilic attack on the C6-carbonyl, catalytic mechanism, overview. BphD is a half-site reactive enzyme with versatility of the Ser-His-Asp triad, role of the catalytic His in acylation and deacylation	719664	
3.7.1.8	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate	general base and nucleophilic catalytic reaction mechanisms, overview	718941	
3.7.1.8	2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate	mechanism may involve an Asp-Ser-His catalytic triad	247043