Carboxymethylproline synthase catalysed syntheses of functionalised N-heterocycles.
The utility of wild-type and variant carboxymethylproline synthases for biocatalysis was demonstrated by preparing functionalised 5-, 6- and 7-membered N-heterocycles from amino acid aldehydes and (alkylated) malonyl-coenzyme A derivatives; the N-heterocycles produced were converted to the corresponding bicyclic beta-lactams by a carbapenem synthetase.
Hamed
Refaat B
RB
University of Oxford, Department of Chemistry, Chemistry Research Laboratory, Mansfield Road, Oxford, UK OX1 3TA.
Mecinović
Jasmin
J
Ducho
Christian
C
Claridge
Timothy D W
TD
Schofield
Christopher J
CJ
D000447:Aldehydes / Q000737:chemistry; D001665:Binding Sites; D055162:Biocatalysis; D019755:Carbon-Carbon Lyases / Q000378:metabolism*; D019731:Carbon-Nitrogen Ligases / Q000378:metabolism; D018360:Crystallography, X-Ray; D006571:Heterocyclic Compounds / Q000737:chemistry / Q000378:metabolism*; D008316:Malonyl Coenzyme A / Q000737:chemistry; D011487:Protein Conformation; D047090:beta-Lactams / Q000737:chemistry / Q000378:metabolism
D000447:Aldehydes; D006571:Heterocyclic Compounds; D047090:beta-Lactams; D008316:Malonyl Coenzyme A; D019755:Carbon-Carbon Lyases; C484323:carboxymethylproline synthase; D019731:Carbon-Nitrogen Ligases; C479139:carbapenam synthetase