An unusual matrix of stereocomplementarity in the hydroxylation of monohydroxy fatty acids catalysed by cytochrome P-450 from Bacillus megaterium with potential application in biotransformations

Cytochrome P450 from Bacillus megaterium catalyses the diastereoselective hydroxylations of 13-hydroxymyristic acid, to predominantly erythro-12,13-dihydroxymyristic acid, and of 12-hydroxymyristic acid to give predominantly threo-12,13-dihydroxymyristic acid, in reactions that are stereocomplementary and with considerable potential application in biotransformations.

[1]  J Deisenhofer,et al.  Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. , 1993, Science.

[2]  J. S. Miles,et al.  Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization. , 1992, The Biochemical journal.

[3]  L. Narhi,et al.  Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. , 1986, The Journal of biological chemistry.

[4]  C. Wong,et al.  Enzymatic catalysis in organic synthesis. , 1991, Methods in enzymology.

[5]  T. Poulos,et al.  High-resolution crystal structure of cytochrome P450cam. , 1987, Journal of molecular biology.

[6]  G. Whitesides,et al.  Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration by using glucose-6-phosphate and the glucose-5-phosphate dehydrogenase from Leuconostoc mesenteroides , 1981 .

[7]  Y. Koga,et al.  Excess partial molar enthalpies in the water-rich region of the isobutyric acid – water system , 1991 .

[8]  G. Whitesides,et al.  Laboratory-scale enzymic/chemical syntheses of D- and L-.beta.-chlorolactic acid and D- and L-potassium glycidate , 1982 .

[9]  J. Falck,et al.  The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3* , 1996, The Journal of Biological Chemistry.

[10]  J. Holbrook,et al.  D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. II. Mutagenic analysis of catalytically important residues. , 1997, European journal of biochemistry.