Rhodococcus jostii

Rosloniec KZ, Wilbrink MH, Capyk JK, Mohn WW, Ostendorf M, van der Geize R, Dijkhuizen L, Eltis LD (2009) Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHAl. Mol Microbiol 74 1031-1043... 

A. Riebel, G. de Gonzalo, M.W. Fraaije, Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHAl,). Mol. Catal B. Enzym. 88 (2013) 20-25. 

Nitrile hydratases (NHases) exhibit broader substrate specificities than nitrilases, and they are more tolerant of sterically demanding substrates. In contrast, NHases mainly exhibit lower enantioselectivities than nitrilases, although biotransformations of a few specific nitriles by NHase proceeded with excellent enantioselectivities [5,6]. Low NHase enantioselectivity, however, can be compensated for by using enantiose-lective amidases in the next step. NHases are usually less thermostable than nitrilases, but a few of them are resistant to increased temperatures or organic solvent concentrations [8, 9]. The majority of characterized NHases are Fe or Co type, except for a new NHase with three metal ions (Co, Cu, Zn) reported in Rhodococcus jostii [85]. 

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