Abstract
Cytochrome P450 (CYP) monooxygenases, the nature’s most versatile biological catalysts have unique ability to catalyse regio-, chemo-, and stereospecific oxidation of a wide range of substrates under mild reaction conditions, thereby addressing a significant challenge in chemocatalysis. Though CYP enzymes are ubiquitous in all biological kingdoms, the divergence of CYPs in fungal kingdom is manifold. The CYP enzymes play pivotal roles in various fungal metabolisms starting from housekeeping biochemical reactions, detoxification of chemicals, and adaptation to hostile surroundings. Considering the versatile catalytic potentials, fungal CYPs has gained wide range of attraction among researchers and various remarkable strategies have been accomplished to enhance their biocatalytic properties. Numerous fungal CYPs with multispecialty features have been identified and the number of characterized fungal CYPs is constantly increasing. Literature reveals ample reviews on mammalian, plant and bacterial CYPs, however, modest reports on fungal CYPs urges a comprehensive review highlighting their novel catalytic potentials and functional significances. In this review, we focus on the diversification and functional diversity of fungal CYPs and recapitulate their unique and versatile biocatalytic properties. As such, this review emphasizes the crucial issues of fungal CYP systems, and the factors influencing efficient biocatalysis.
Highlights
Cytochrome P450 (CYP) monooxygenases, the ubiquitous enzymes with catalytic versatility, substrate diversity and atypical kinetics are one of the most fascinating targets for biocatalysis and play diverse roles in biotechnology, medicine and bioremediation [1,2,3]
Functionomic studies carried out with 425 CYP isoforms from P. chrysosporium (120 CYPs), P. placenta (184 CYPs), and A. oryzae (121 CYPs) using S. cerevisiae cytochrome P450 reductase (CPR) resulted in the discovery of several CYPs with novel catalytic potentials (Fig. 4) [18, 82]
Significance of CPR in fungal CYP‐mediated reactions Cytochrome P450 reductase, the membrane-bound diflavin electron donor protein, is crucial for CYP mediated reactions as it is responsible for the sequential delivery of two electrons for the activation of molecular oxygen in the class II system [29]
Summary
Cytochrome P450 (CYP) monooxygenases, the ubiquitous enzymes with catalytic versatility, substrate diversity and atypical kinetics are one of the most fascinating targets for biocatalysis and play diverse roles in biotechnology, medicine and bioremediation [1,2,3]. Functional diversity of fungal CYPs In the fungal kingdom, CYPs are involved in the biosynthesis of various primary and secondary metabolites with high substrate specificity. The chemically complex stereoand regioselective hydroxylation steps involved in the production of steroid drugs are performed by certain filamentous fungi mediated by CYP enzymes [54].
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