Highly efficient synthesis of 5‐cyanovaleramide by <i>Rhodococcus ruber</i> CGMCC3090 resting cells

Shen, Yanbing; Li, Xiaodan; Zhang, Jinli; Hua, Sun; Luo, Jianmei

doi:10.1002/jctb.3756

Cited by 18 publications

(13 citation statements)

References 13 publications

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“…The following solvent system was used: 25 m m H 3 PO 4 buffer (pH 2.5) and methanol (89.01:10.09 vol/vol) at 1 mL min −1 . A wavelength of 210 nm was used for monitoring . The kinetic parameters for 5‐CVAM and CAAM hydration by NHases were determined in 10 m m KPB at 35 °C for 3 min, and the concentration of the enzyme was 0.3 mg mL −1 .…”

Section: Methodsmentioning

confidence: 99%

Modulation of Nitrile Hydratase Regioselectivity towards Dinitriles by Tailoring the Substrate Binding Pocket Residues

et al. 2017

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The regioselective hydration of dinitriles is one of the most attractive approaches to prepare ω‐cyanocarboxamides or diamides and such regioselectivity is often beyond the capability of chemical catalysts. The use of nitrile hydratase to biotransform dinitriles selectively would be highly desirable. Molecular docking of two aliphatic dinitriles and two aromatic dinitriles into the active site of a nitrile hydratase (NHase) from Rhodococcus rhodochrous J1 allowed the identification of proximal NHase substrate binding pocket residues. Four residues (βLeu48, βPhe51, βTyr68, and βTrp72) were selected for single‐ and double‐point mutations to modulate the NHase regioselectivity towards dinitriles. Several NHase mutants with an altered regioselectivity were obtained, and the best one was Y68T/W72Y. Docking experiments further indicated that the poor binding affinity of aliphatic and aromatic ω‐cyanocarboxamides to the NHase variants resulted in distinct regioselectivity between wild‐type and mutated NHases.

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Section: Methodsmentioning

confidence: 99%

Modulation of Nitrile Hydratase Regioselectivity towards Dinitriles by Tailoring the Substrate Binding Pocket Residues

et al. 2017

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“…were shown to convert fluorinated aromatic dinitriles [137] and R. rhodochrous IFO 15564 was active toward alicyclic mono- and dinitriles, affording the products in low to moderate yields [138]. Resting cells of R. ruber CGMCC3090 converted the aliphatic adiponitrile to selectively give 5-cyanovaleramide (5-CVAM), which is used in the synthesis of caprolactam, a common precursor for Nylon 6 (Scheme 14) [139].…”

Section: Enzymes From the Aldoxime-nitrile Pathwaymentioning

confidence: 99%

Rhodococcus as a Versatile Biocatalyst in Organic Synthesis

Busch

Hagedoorn

Hanefeld

2019

IJMS

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The application of purified enzymes as well as whole-cell biocatalysts in synthetic organic chemistry is becoming more and more popular, and both academia and industry are keen on finding and developing novel enzymes capable of performing otherwise impossible or challenging reactions. The diverse genus Rhodococcus offers a multitude of promising enzymes, which therefore makes it one of the key bacterial hosts in many areas of research. This review focused on the broad utilization potential of the genus Rhodococcus in organic chemistry, thereby particularly highlighting the specific enzyme classes exploited and the reactions they catalyze. Additionally, close attention was paid to the substrate scope that each enzyme class covers. Overall, a comprehensive overview of the applicability of the genus Rhodococcus is provided, which puts this versatile microorganism in the spotlight of further research.

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“…They have activity against a broad range of nitriles, including phenylacetonitrile, 2phenylpropionitrile, 2-phenylglycinonitrile, mandelonitrile, 2-phenylbutyronitrile, 3-phenylpropionitrile, N-phenylglycinonitrile, p-toluonitrile and 3-hydroxy-3-phenylpropionitrile [33]. R. ruber CGMCC3090 and other strains express nitrile hydratases [116,129] while the nitrile hydrolysis activity of R. hoagii [116] is also attributed to a nitrile hydratase [130].…”

Section: Nitrile Conversionmentioning

confidence: 99%

The complete genome sequence of the nitrile biocatalyst Rhodocccus rhodochrous ATCC BAA-870

Frederick

Hennessy

Horn

et al. 2019

Preprint

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Background Rhodococci are industrially important soil-dwelling Gram-positive bacteria that are well known for both nitrile hydrolysis and oxidative metabolism of aromatics. Rhodococcus rhodochrous ATCC BAA-870 is capable of metabolising a wide range of aliphatic and aromatic nitriles and amides. The genome of the organism was sequenced and analysed in order to better understand this whole cell biocatalyst. Results The genome of R. rhodochrous ATCC BAA-870 is the first Rhodococcus genome fully sequenced using Nanopore sequencing. The circular genome contains 5.9 megabase pairs (Mbp) and includes a 0.53 Mbp linear plasmid, that together encode 7548 predicted protein sequences according to BASys annotation, and 5535 predicted protein sequences according to RAST annotation. The genome contains numerous oxidoreductases, 15 identified antibiotic and secondary metabolite gene clusters, several terpene and nonribosomal peptide synthetase clusters, as well as 6 putative clusters of unknown type. The 0.53 Mbp plasmid encodes 677 predicted genes and contains the nitrile converting gene cluster, including a nitrilase, a low molecular weight nitrile hydratase, and an enantioselective amidase. Although there are fewer biotechnologically relevant enzymes compared to those found in rhodococci with larger genomes, such as the well-known Rhodococcus jostii RHA1, the abundance of transporters in combination with the myriad of enzymes found in strain BAA-870 might make it more suitable for use in industrially relevant processes than other rhodococci. Conclusions The sequence and comprehensive description of the R. rhodochrous ATCC BAA-870 genome will facilitate the additional exploitation of rhodococci for biotechnological applications, as well as enable further characterisation of this model organism. The genome encodes a wide range of enzymes, many with unknown substrate specificities supporting potential applications in biotechnology, including nitrilases, nitrile hydratase, monooxygenases, cytochrome P450s, reductases, proteases, lipases, and transaminases.

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Highly efficient synthesis of 5‐cyanovaleramide by Rhodococcus ruber CGMCC3090 resting cells

Cited by 18 publications

References 13 publications

Modulation of Nitrile Hydratase Regioselectivity towards Dinitriles by Tailoring the Substrate Binding Pocket Residues

Modulation of Nitrile Hydratase Regioselectivity towards Dinitriles by Tailoring the Substrate Binding Pocket Residues

Rhodococcus as a Versatile Biocatalyst in Organic Synthesis

The complete genome sequence of the nitrile biocatalyst Rhodocccus rhodochrous ATCC BAA-870

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