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Beard, Timothy M.; Page, Michael I.

doi:10.1023/a:1001712230455

Cited by 26 publications

(5 citation statements)

References 5 publications

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“…The cobalt NHase activity from R. rhodochrous J1, like that of the iron containing NHase from R. erythropolis, is able to hydrate aliphatic nitrile compounds but has been reported to have higher activity against aromatic compounds [11]. Apart from the nitrile hydratase and an associated amidase [12,13], Rhodococci also express a competing nitrilase that generates the corresponding carboxylic acid [14]. This creates a complication when analysing the nitrile hydratase activity using whole cells [15,16] as both pathways can result in either carboxamides or carboxylic acid products, depending on the substrate [17].…”

Section: Introductionmentioning

confidence: 99%

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

et al. 2020

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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.

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Section: Introductionmentioning

confidence: 99%

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

et al. 2020

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“…Along with nitrile hydratases, amidases can catalyze the unique conversion of nitriles to the corresponding enantiopure carboxylic acids. Rhodococcal amidase and nitrile hydratase find applications in the stereoselective synthesis of several drugs and drug intermediates 3,36 . Hence, large scale fermentative production of Rhodococcal amidase is of great commercial interest.…”

Section: Introductionmentioning

confidence: 99%

Enhanced Production of Acyltransferase from Rhodococcus pyridinivorans using Statistical Experimental Design

Devi,

Kumari,

Lata

et al. 2017

J. Adv. Mircobiol.

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Optimization of growth parameters for enhanced production of acyltransferase byRhodococcus pyridinivorans were carried out using one-variable-at-a-time strategy (OVAT) and statistical designs of response surface methodology (RSM) to describe the relationship between tested variables. Optimization resulted into 3.8 folds increase in the acyltransferase production (448.44 ± 7.00 Umg -1 dcw). Based on results of Plackett-Burman design, combined effect of variables viz. pH, temperature, inoculum size and nonsubstrate inducer acetonitrile on production of acyltransferase were investigated at four levels, through the statistical analysis of central composite design (CCD). The statistical optimization showed further increase in acyltransferase activity of 1.06 folds. The validation of the experiments was also done by point determination in generated model with actual and predicted response level under optimized condition which resulted acyltransferase production of 480.8 ± 2.01 U mg -1 dcw (Predicted response 474.71 U mg -1 dcw). After performing optimization of all production parameters, 4.2 fold increase in acyltransferase production (519.03 ± 1.093 U mg -1 dcw) was recorded with 3.0 % (w/v) acetamide, 1.5 % (w/v) yeast extract, 0.5 % (w/v) NaCl, 0.2 % (w/v) glucose, pH 7.0 at 30°C, 8 % (v/v) inoculum size and acetonitrile in multistep feeding as non substrate inducer (70 mM) for 18 h.

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“…Bacteria from different genera, including Rhodococcus , possess similar enzyme systems and alk -genes (Whyte et al 1998; Whyte et al 2002). Members of the genus Rhodococcus seem to play significant role in bioremediation of oil spills (Whyte et al 2002) and are recognized as ideal candidates for the biodegradation of hydrocarbons due to their ability to degrade a wide range of organic compounds (Beard and Page 1998), their hydrophobic cell surface and the production of biosurfactants as well as their ubiquity and robustness in the environment (Larkin et al 1998; Warhurst and Fewson 1994). …”

Section: Introductionmentioning

confidence: 99%

The complete alk sequences of Rhodococcus erythropolis from Lake Baikal

2014

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BackgroundRhodococci are bacteria able to degrade a wide range of hydrocarbons, including the alkanes present in crude oil, due to alk genes in their genomes.FindingsGenome sequencing of DNA from Rhodococcus erythropolis strain 4 (obtained from a deep-water bitumen mound) revealed four alk genes, and the predicted amino acid sequences coded by these genes were highly conserved, having sections up to 11 amino acid residues.ConclusionsObtained four genes from Rhodococcus erythropolis were similar to corresponding genes from other bacteria collected from other environments, including marine sources. This indicated a large-scale horizontal alk gene transfer between bacteria from different subgenera.

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Cited by 26 publications

References 5 publications

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

Substrate Profiling of the Cobalt Nitrile Hydratase from Rhodococcus rhodochrous ATCC BAA 870

Enhanced Production of Acyltransferase from Rhodococcus pyridinivorans using Statistical Experimental Design

The complete alk sequences of Rhodococcus erythropolis from Lake Baikal

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