An article Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870 WOS:000513770000238 published article about ENANTIOSELECTIVE BIOTRANSFORMATIONS; INDUSTRIAL-PRODUCTION; J1; HYDROLYSIS; REGIOSELECTIVITY; PURIFICATION; BENZONITRILE; DINITRILES; INSIGHTS; AMIDASE in [Mashweu, Adelaide R.; Chhiba-Govindjee, Varsha P.; Bode, Moira L.; Brady, Dean] Univ Witwatersrand, Sch Chem, Mol Sci Inst, ZA-2050 Johannesburg, South Africa; [Chhiba-Govindjee, Varsha P.] CSIR Chem Prod Cluster, POB 395, ZA-0001 Pretoria, South Africa in 2020, Cited 41. The Name is 2-Aminobenzamide. Through research, I have a further understanding and discovery of 88-68-6. Application In Synthesis of 2-Aminobenzamide
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-Bienayme 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-Bienayme 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.
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