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http://purl.uniprot.org/citations/27411040http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27411040http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27411040http://www.w3.org/2000/01/rdf-schema#comment"Three enzymes of the Mentha essential oil biosynthetic pathway are highly homologous, namely the ketoreductases (-)-menthone:(-)-menthol reductase and (-)-menthone:(+)-neomenthol reductase, and the "ene" reductase isopiperitenone reductase. We identified a rare catalytic residue substitution in the last two, and performed comparative crystal structure analyses and residue-swapping mutagenesis to investigate whether this determines the reaction outcome. The result was a complete loss of native activity and a switch between ene reduction and ketoreduction. This suggests the importance of a catalytic glutamate vs. tyrosine residue in determining the outcome of the reduction of α,β-unsaturated alkenes, due to the substrate occupying different binding conformations, and possibly also to the relative acidities of the two residues. This simple switch in mechanism by a single amino acid substitution could potentially generate a large number of de novo ene reductases."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.org/dc/terms/identifier"doi:10.1002/anie.201603785"xsd:string
http://purl.uniprot.org/citations/27411040http://purl.org/dc/terms/identifier"doi:10.1002/anie.201603785"xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Leys D."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Leys D."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Scrutton N.S."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Scrutton N.S."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Toogood H.S."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Toogood H.S."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Gardiner J.M."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Gardiner J.M."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Karuppiah V."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Karuppiah V."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Ni Cheallaigh A."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Ni Cheallaigh A."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Hoeven R."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Hoeven R."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Lygidakis A."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/author"Lygidakis A."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/name"Angew. Chem. Int. Ed."xsd:string
http://purl.uniprot.org/citations/27411040http://purl.uniprot.org/core/name"Angew Chem Int Ed Engl"xsd:string