Mashweu, ARBode, MLBrady, DChhiba, Varsha P2020-07-272020-07-272020Mashweu, A.R. (et.al.) 2020. Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870. Molecules, v25(1), 238, 16pp.1420-3049https://www.mdpi.com/1420-3049/25/1/238https://pubmed.ncbi.nlm.nih.gov/31935987/https://doi.org/10.3390/molecules25010238http://hdl.handle.net/10204/11511Copyright: 2020 MDPI. This is the full text version of the work.The aromatic substrate profile of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da) to large (325 Da) were evaluated. Larger compounds included those with a bi-aryl axis, prepared by the Suzuki coupling reaction, Morita–Baylis–Hillman adducts, heteroatom-linked diarylpyridines prepared by Buchwald–Hartwig cross-coupling reactions and imidazo[1,2- a]pyridines prepared by the Groebke–Blackburn–Bienaymé multicomponent reaction. The enzyme active site was moderately accommodating, accepting almost all of the small aromatic nitriles, the diarylpyridines and most of the bi-aryl compounds and Morita–Baylis–Hillman products but not the Groebke–Blackburn–Bienaymé products. Nitrile conversion was influenced by steric hindrance around the cyano group, the presence of electron donating groups (e.g., methoxy) on the aromatic ring, and the overall size of the compound.enGreen chemistryNitrile hydrataseBiocatalysisCarboxamideArticleMashweu, A., Bode, M., Brady, D., & Chhiba, V. P. (2020). Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870. http://hdl.handle.net/10204/11511Mashweu, AR, ML Bode, D Brady, and Varsha P Chhiba "Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870." (2020) http://hdl.handle.net/10204/11511Mashweu A, Bode M, Brady D, Chhiba VP. Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870. 2020; http://hdl.handle.net/10204/11511.TY - Article AU - Mashweu, AR AU - Bode, ML AU - Brady, D AU - Chhiba, Varsha P AB - The aromatic substrate profile of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da) to large (325 Da) were evaluated. Larger compounds included those with a bi-aryl axis, prepared by the Suzuki coupling reaction, Morita–Baylis–Hillman adducts, heteroatom-linked diarylpyridines prepared by Buchwald–Hartwig cross-coupling reactions and imidazo[1,2- a]pyridines prepared by the Groebke–Blackburn–Bienaymé multicomponent reaction. The enzyme active site was moderately accommodating, accepting almost all of the small aromatic nitriles, the diarylpyridines and most of the bi-aryl compounds and Morita–Baylis–Hillman products but not the Groebke–Blackburn–Bienaymé products. Nitrile conversion was influenced by steric hindrance around the cyano group, the presence of electron donating groups (e.g., methoxy) on the aromatic ring, and the overall size of the compound. DA - 2020 DB - ResearchSpace DP - CSIR KW - Green chemistry KW - Nitrile hydratase KW - Biocatalysis KW - Carboxamide LK - https://researchspace.csir.co.za PY - 2020 SM - 1420-3049 T1 - Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 TI - Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 UR - http://hdl.handle.net/10204/11511 ER -