Rhodococcus rhodochrous

MacMichael GJ, LR Brown (1987) Role of carbon dioxide in catabolism of propane by Nocardia parafflni-cum (Rhodococcus rhodochrous). Appl Environ Microbiol 53 65-69. 

Simoni S, S Klinke, C Zipper, W Angst, H-P E Kohler (1996) Enantioselective metabolism of chiral 3-phenyl-butyric acid, an intermediate of linear alkylbenzene degradation, by Rhodococcus rhodochrous. Appl... 

Toraya T, T Oka, M Ando, M Yamanishi, H Nishihara (2004) Novel pathway for utilization of cycloropanecar-boxylate by Rhodococcus rhodochrous. Appl Environ Microbiol 70 224-228. 

The oxidation of f-butyl methyl ether to f-butanol (Steffan et al. 1997), which is also mediated by the cytochrome P450 from camphor-grown Pseudomonas putida CAM, but not by that from Rhodococcus rhodochrous strain 116. 

Karlson U, DF Dwyer, SW Hooper, ERB Moore, KN Timmis, LD Eltis (1993) Two independently regulated cytochromes P-450 in a Rhodococcus rhodochrous strain that degrades 2-ethoxyphenol and 4-methoxybenzoate. J Bacterial 175 1467-1474. 

In the hydroxylation of n-propane to n-propanol by Nocardia paraffinicum (Rhodococcus rhodochrous) ATCC 21198, the ratio of hydrocarbon to oxygen consumed was 2 1 and this suggests that the reaction of two molecules of propane and one molecule of dioxygen... 

Warhurst AM, KF Clarke, RA Hill, RA Holt, CA Fewson (1994) Metabolism of styrene by Rhodococcus rhodochrous NCIMB 13259. Appl Environ Microbiol 60 1137-1145. 

Cyclopropane carboxylic acid is degraded via 3-hydroxybutyrate by both the bacterium Rhodococcus rhodochrous (Toraya et al. 2004) (Figure 7.33) and by fungi (Schiller and Chung 1970), although the mechanism for ring fission has not been determined. 

Curragh H, O Flynn, MJ Larkin, TM Stafford, JTG Hamilton, DB Harper (1994) Haloalkane degradation and assimilation by Rhodococcus rhodochrous NCIMB 13064. Microbiology (UK) 140 1433-1442. 

Fuchs K, A Schreiner, F Lingens (1991) Degradation of 2-methylaniline and chlorinated isomers of 2-methyl-aniline by Rhodococcus rhodochrous strain CTM. J Gen Microbiol 137 2033-2039. 

Haroune N, B Combourieu, P Besse, M Sancelme, A Kloepfer, T Reemtsma, H De Wever, A-M Delort (2004) Metabolism of 2-mercaptobenzothiazole by Rhodococcus rhodochrous. Appl Environ Microbiol 70 6315-6319. 

The enantiomeric reduction of 2-nitro-l-phenylprop-l-ene has been studied in a range of Gram-positive organisms including strains of Rhodococcus rhodochrous (Sakai et al. 1985). The enantiomeric purity of the product depended on the strain used, the length of cultivation, and the maintenance of a low pH that is consistent with the later results of Meah and Massey (2000). It has been shown that an NADPH-linked reduction of a,p-unsaturated nitro compounds may also be accomplished by old yellow enzyme via the flcf-nitro form (Meah and Massey 2000). This is formally analogous to the reduction and dismutation of cyclic enones by the same enzyme (Vaz et al. 1995), and the reductive fission of nitrate esters by an enzyme homologous to the old yellow enzyme from Saccharomyces cerevisiae (Snape et al. 1997). 

Seth-Smith HMB, SJ Rosser, A Basran, ER Travis, ER Dabbs, S Nicklin, NC Bruce (2002) Cloning, sequencing, and characterization of the hexahydro-l,3,5-trinitro-l,3,5-triazine degradation gene cluster from Rhodococcus rhodochrous. Appl Environ Microbiol 68 4764-4771. 

Nagasawa, T., Shimizu, H. and Yamada, H. (1993) The superiority of the third-generation catalyst, Rhodococcus rhodochrous J1 nitrile hydratase, for industrial production of acrylamide. AppliedMircobiology and Biotechnology, 40, 189-195. 

Table 8.1 Temperature stability of Rhodococcus rhodochrous J1E/393G mutant NHase compared with J1 NHase, each expressed in Escherichia coli JM109...

Acrylonitrile produced industrially via propylene ammoxidation contains trace amounts of benzene. When using Pseudonocardia thermophila JCM3095 or Rhodococcus rhodochrous J-1 as microbial NHase catalyst for conversion of acrylonitrile to acrylamide, concentrations of benzene of <4 ppm produced a significant increase in the reaction rate [16]. Maintaining the concentration of HCN and oxazole at <5 ppm and <10 ppm respectively produced high-quality acrylamide suitable for polymerization. 

While the production of acrylamide by NHase is a well-established industrial process, only a first report exists for the production of butyramide from butyronitrile. Using Rhodococcus rhodochrous PA-34 (at a loading of 1 g dew), 595 g butyramide was prepared in quantitative yield from 60% (v/v) butyronitrile in a pH 7.0, 1 L batch reaction, at 10 °C [18]. 

Table 8.2 Comparison of the thermal stability of NHase activities of Rhodococcus sp. FZ4 and GF270 to Amycolatopsis sp. NA40 and Rhodococcus rhodochrous J1 ...

Rhodococcus sp. GF270 Amycolatopsis sp. NA40 Rhodococcus rhodochrous Jl ... 

The activities of NHases from Rhodococcus sp. Adpl2 and Gordonia sp. BR-1 strains have been partially characterized [25]. In reactions that catalyze the hydration of a-hydroxynitriles such as lactonitrile or glycolonitrile, the substrate can dissociate to produce HCN and the corresponding aldehydes. HCN can inhibit and/or inactivate NHase, and it was determined that these two enzymes remain active in the presence of cyanide ion at concentrations up to 20 him. The dependence of the NHase activity of cell-free extracts of Rhodococcus rhodochrous J1 and Gordonia sp. BR-1 on cyanide ion concentration is illustrated in Figure 8.1, demonstrating the improved cyanide stability of BR-1 NHase relative to that of Jl. 

Figure 8.1 Dependence of the NHase activity of cell-free extracts of Rhodococcus rhodochrous J1 (a) and Gordonia sp. BR-1 ( ) on cyanide ion concentration...

The NHase and amidase from Rhodococcus rhodochrous IFO 15 564 was studied using a series of a,a-disubstituted malononitriles. This amidase preferentially hydrolyzes the pro (R) amide of the prochiral di-amide, which is an intermediate resulting from the nonenantiotopic NHase activity on the dinitrile substrate. This transformation was combined with a Hofmann rearrangement to generate a key precursor of (A)-methyldopa in 98.2% ee and 95% yield (Figure 8.5) [41],... 

The regioselectivity of a Rhodococcus rhodochrous nitrilase has been demonstrated for the conversion of 5-fluoro-l,3-dicyanobenzene to 5-fluoro-3-cyano-benzoic acid [62]. The nitrilase was expressed in an Escherichia coli transformant, and a cell-free extract was employed as catalyst (0.14wt% cell-free extract) in 0.1m sodium phosphate buffer (pH 7.2) at 25 °C containing 0.18 m 5-fluoro-l,3-dicyanobenzene. After 72 h, the conversion was >98% and the reaction was stopped by addition of phosphoric acid (pH 2.4) to yield 5-fluoro-3-cyano-benzoic acid as a crystalline product (97% isolated yield). 

The preparation of malonic acid monoesters has been demonstrated using the microbial nitrilase activity of Corynebacterium nitrilophilus ATCC 21 419, Gordona terrae MA-1, or Rhodococcus rhodochrous ATCC 33 025 to hydrolyze methyl cyanoacetate, ethyl cyanoace-tate, M-propyl cyanoacetate, isopropyl cyanoacetate, M-butyl cyanoacetate, tertbutyl cyanoacetate, 2-ethylhexyl cyanoacetate, allyl cyanoacetate, and benzyl cyanoacetate [96]. By maintaining the concentration of nitrile in a reaction mixture at <5 wt%, significant inactivation of the nitrilase activity was avoided for example, a total of 25 g of M-propyl cyanoacetate was added in sequential 5g portions to a lOOmL suspension of Rhodococcus rhodochrous ATCC 33 025 cells (OD630 = 5.6) in 50 mM phosphate buffer (pH 7.0) over 30h at 25 °C to produce mono-M-propyl malonate in 100% yield (Figure 8.17). 

Figure 8.17 Production of mono-n-propyl malonate from M-propyl cyanoacetate using the microbial nitrilase activity of Rhodococcus rhodochrous ATCC 33025...

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