Rhodococcus ruber

Kostichka K, SM Thomas, KJ Gibson, V Nagarajan, Q Cheng (2001) Cloning and characterization of a gene cluster for cyclododecanone oxidation in Rhodococcus ruber SCI. J Bacterial 183 6478-6486. 

Cyclododecanone monooxygenase from Rhodococcus ruber SCI is different from those already mentioned, and is active towards substrates with more than seven carbon atoms (Kostichka et al. 2001). 

The reduction of several ketones, which were transformed by the wild-type lyophilized cells of Rhodococcus ruber DSM 44541 with moderate stereoselectivity, was reinvestigated employing lyophilized cells of Escherichia coli containing the overexpressed alcohol dehydrogenase (ADH- A ) from Rhodococcus ruber DSM 44541. The recombinant whole-cell biocatalyst significantly increased the activity and enantioselectivity [41]. For example, the enantiomeric excess of (R)-2-chloro-l-phenylethanol increased from 43 to >99%. This study clearly demonstrated the advantages of the recombinant whole cell biocatalysts over the wild-type whole cells. 

Stampfer, W., Kosjek, B., Faber, K. and Kroutil, W. (2003) Biocatalytic asymmetric hydrogen transfer employing Rhodococcus ruber DSM 44541. The Journal of Organic Chemistry, 68 (2), 402-406. 

Van Deursen, R., Stampfer, W., Edegger, K. et al. (2004) Chemo- and stereo-selective biocatalytic reduction of a,/8-unsaturated ketones employing a chemo-tolerant ADH from Rhodococcus ruber DSM 44541. Journal of Molecular Catalysis B-Enzymatic, 31 (4-6), 159-163. 

Pseudomonas oleovorans (PhaC2) —Nocardia corallina ----Rhodococcus ruber PP2... 

The 3-ketothiolase has been purified and investigated from several poly(3HB)-synthesizing bacteria including Azotobacter beijerinckii [10], Ral-stonia eutropha [11], Zoogloea ramigera [12], Rhodococcus ruber [13], and Methylobacterium rhodesianum [14]. In R. eutropha the 3-ketothiolase occurs in two different forms, called A and B, which have different substrate specificities [11,15]. In the thiolytic reaction, enzyme A is only active with C4 and C5 3-ketoacyl-CoA whereas the substrate spectrum of enzyme B is much broader, since it is active with C4 to C10 substrates [11]. Enzyme A seems to be the main biosynthetic enzyme acting in the poly(3HB) synthesis pathway, while enzyme B should rather have a catabolic function in fatty-acid metabolism. However, in vitro studies with reconstituted purified enzyme systems have demonstrated that enzyme B can also contribute to poly(3HB) synthesis [15]. 

In Rhodococcus ruber and Nocardia corallina the polymers composed of 3-hydroxybutyryl and 3-hydroxyvaleryl residues are synthesized from sugars by methyl-malonyl-CoA. Succinyl-CoA is decarboxylated via methyl-malonyl-CoA to propionyl-CoA as the precursor of 3-hydroxyvaleryl-CoA [40]. 

Overall, retaining sec-alkylsulfatase activity has been detected in Planctomycetes spp. (such as Rhodopirellula baltica DSM 10527 complementary inverting sulfatase activity was found in Actinomycetes (e.g. Rhodococcus ruber DSM 44541 " ), Archaea (e.g. Sulfolobus spp. ) and pseudomonads. ... 

Pseudomonas spp. DSM 6611 and 6978 and Rhodococcus ruber DSM 44541 were obtained from DSMZ (Deutsche Stammsammlung fiir Mikroorganismen und Zellkulturen, Braunschweig, Germany, www.dsmz.de)... 

Pogorevc, M. and Faber, K., Enantioselective stereoinversion of rec-alkyl sulfates by an alkyl-sulfatase from Rhodococcus ruber DSM 44541. Tetrahedron Asymm., 2002,13, 1435. 

Organisms Lactobacillus kefir DSM 20587, Saccharomyces cerevisiae, Candida magnoliae, Bacillus megaterium, Thermoanaerobium brockii, Clostridium beijerinckii, Thermoanaerobacter ethanolicus, Rhodococcus ruber DSM 44541. Solvents ace = acetone iPr = i-PrOH. Substrates WM Wieland-Miescher ketone 4-Me-HP 4-methyl Hajos-Parrish ketone COBE ethyl 4-chloro-3-oxobutanoate. 

W. Stampfer, B. Kosjek, W. Kroutil, and K. Faber, On the organic solvent and thermostability of the biocatalytic redox system of Rhodococcus ruber DSM 44541, Biotechnol. Bioeng. 2003a, 81, 865-869. 

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