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emi12108-sup-0001-tables1.docx25K

Table S1. Bacterial strains and plasmids used in this study.

emi12108-sup-0002-tables2.docx25K

Table S2. Primers used in this study.

emi12108-sup-0003-figs1.docx101K

Fig. S1. Genomic structure of the CYP125 and CYP142 regions in M. tuberculosis and M. smegmatis mc2 155. Comparison of chromosomal regions flanking the genes encoding cytochromes CYP142 (A) and CYP125 (B). The details of ORFs (open reading frames) and the amino acid sequence identity are listed in Table 1. The arrows indicate direction of transcription.

emi12108-sup-0004-figs2.docx694K

Fig. S2. Binding of inhibitors to purified CYP125A3 and CYP142A2. The dependence of the absorbance change of CYP12A35 (column A) and CYP142A2 (column B) at 418 nm induced by the different inhibitor molecules tested (indicated in the figure). The best fit of Eq. (1) (see Experimental procedures) is represented as a black line.

emi12108-sup-0005-figs3.docx586K

Fig. S3. Fragmentation pattern of the products of the CYP125A3 and CYP142A2-catalysed transformation of 4-cholesten-3-one. LC-MS data include the compound name, chemical structure, chromatographic retention times and mass spectra.

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