Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehydes / chemistry
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Binding Sites
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Biocatalysis
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Carbon-Carbon Lyases / metabolism*
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Carbon-Nitrogen Ligases / metabolism
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Crystallography, X-Ray
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Heterocyclic Compounds / chemistry
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Heterocyclic Compounds / metabolism*
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Malonyl Coenzyme A / chemistry
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Protein Conformation
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beta-Lactams / chemistry
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beta-Lactams / metabolism
Substances
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Aldehydes
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Heterocyclic Compounds
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beta-Lactams
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Malonyl Coenzyme A
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Carbon-Carbon Lyases
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carboxymethylproline synthase
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Carbon-Nitrogen Ligases
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carbapenam synthetase