dc.contributor.author |
Mashweu, AR
|
|
dc.contributor.author |
Bode, ML
|
|
dc.contributor.author |
Brady, D
|
|
dc.contributor.author |
Chhiba, Varsha P
|
|
dc.date.accessioned |
2020-07-27T06:48:31Z |
|
dc.date.available |
2020-07-27T06:48:31Z |
|
dc.date.issued |
2020 |
|
dc.identifier.citation |
Mashweu, A.R. (et.al.) 2020. Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870. Molecules, v25(1), 238, 16pp. |
en_US |
dc.identifier.issn |
1420-3049 |
|
dc.identifier.uri |
https://www.mdpi.com/1420-3049/25/1/238
|
|
dc.identifier.uri |
https://pubmed.ncbi.nlm.nih.gov/31935987/
|
|
dc.identifier.uri |
https://doi.org/10.3390/molecules25010238
|
|
dc.identifier.uri |
http://hdl.handle.net/10204/11511
|
|
dc.description |
Copyright: 2020 MDPI. This is the full text version of the work. |
en_US |
dc.description.abstract |
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. |
en_US |
dc.language.iso |
en |
en_US |
dc.publisher |
MDPI |
en_US |
dc.relation.ispartofseries |
Worklist;23588 |
|
dc.subject |
Green chemistry |
en_US |
dc.subject |
Nitrile hydratase |
en_US |
dc.subject |
Biocatalysis |
en_US |
dc.subject |
Carboxamide |
en_US |
dc.title |
Substrate profiling of the cobalt nitrile hydratase from Rhodococcus rhodochrous ATCC BAA 870 |
en_US |
dc.type |
Article |
en_US |
dc.identifier.apacitation |
Mashweu, 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/10204/11511 |
en_ZA |
dc.identifier.chicagocitation |
Mashweu, 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/10204/11511 |
en_ZA |
dc.identifier.vancouvercitation |
Mashweu 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. |
en_ZA |
dc.identifier.ris |
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 -
|
en_ZA |