木质素
愈创木酚
生物转化
化学
松柏醇
生物化学
去甲基化
有机化学
酶
发酵
基因
基因表达
DNA甲基化
作者
S.J.B. Mallinson,Melodie M. Machovina,Rodrigo L. Silveira,Marc Garcia‐Borràs,Nathan M. Gallup,Christopher W. Johnson,Mark D. Allen,Munir S. Skaf,Michael F. Crowley,Ellen L. Neidle,K. N. Houk,Gregg T. Beckham,Jennifer L. DuBois,J.E. McGeehan
标识
DOI:10.1038/s41467-018-04878-2
摘要
Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-derived aromatic compounds, and is often a key bottleneck for both native and engineered bioconversion pathways. Here, we report the comprehensive characterization of a promiscuous P450 aryl-O-demethylase, consisting of a cytochrome P450 protein from the family CYP255A (GcoA) and a three-domain reductase (GcoB) that together represent a new two-component P450 class. Though originally described as converting guaiacol to catechol, we show that this system efficiently demethylates both guaiacol and an unexpectedly wide variety of lignin-relevant monomers. Structural, biochemical, and computational studies of this novel two-component system elucidate the mechanism of its broad substrate specificity, presenting it as a new tool for a critical step in biological lignin conversion.
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