Identification and Application of Enantiocomplementary Lactamases for Vince Lactam Derivatives. Issue 9 (18th July 2014)

• Record Type: Journal Article
• Authors: Assaf, Zeinab; Eger, Elisabeth; Vitnik, Zeljko; Fabian, Walter M. F.; Ribitsch, Doris; Guebitz, Georg M.; Faber, Kurt; Hall, Mélanie
• Is Part Of: ChemCatChem. Volume 6:Issue 9(2014:Sep.)
• Page Start: 2517
• Page End: 2521
• Publication Date: 2014-07-18
• Subjects: Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201402077
• Languages: English
• ISSNs: 1867-3880

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Four enzymes showing hydrolytic activity on derivatives of 2‐azabicyclo[2.2.1]hept‐5‐en‐3‐one (Vince lactam) were successfully identified through analysis of protein crystal structure and amino acid sequence alignments. Enantiocomplementary activities were observed on Vince lactam and its saturated analog 2‐azabicyclo[2.2.1]heptan‐3‐one with non‐heme chloroperoxidase (CPO‐T) from <italic>Streptomyces aureofaciens</italic>, cyclic imide hydrolase (CIH) from <italic>Pseudomonas putida</italic>, polyamidase (NfpolyA) from <italic>Nocardia farcinica</italic>, and amidase (AMI) from <italic>Rhodococcus globerulus</italic>, and perfect kinetic resolution was achieved (<italic>E</italic>&gt;200). Computational analysis of amide bond resonance stabilization in lactams correlated well with the overall reactivity pattern of the lactams as a function of ring size and strain. The biocatalysts cloned and investigated in this study could be of interest for the synthesis of enantiopure carbocyclic nucleoside analogues.</p> </abstract>