Characterization of a cytochrome P450 that catalyzes the O-demethylation of lignin-derived benzoates.

ABSTRACT: Cytochromes P450 (P450s) are a superfamily of heme-containing enzymes possessing a broad range of monooxygenase activities. One such activity is O-demethylation, an essential and rate-determining step in emerging strategies to valorize lignin that employ carbon-carbon bond cleavage. We recently identified PbdA, a P450 from Rhodococcus jostii RHA1, and PbdB, its cognate reductase, which catalyze the O-demethylation of para-methoxylated benzoates (p-MBAs) to initiate growth of RHA1 on these compounds. PbdA had the highest affinity (K_d = 3.8 ± 0.6 μM) and apparent specificity (k_cat/K_M = 20,000 ± 3000 M^-1 s^-1) for p-MBA. The enzyme also O-demethylated two related lignin-derived aromatic compounds with remarkable efficiency: veratrate and i

SUBMITTER: Wolf ME 

PROVIDER: S-EPMC11530827 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature