Byssochlamys spectabilis (anamorph: Paecilomyces variotii) VdtD Dirigent Protein
Comment
This protein related to lipases is a dirigent protein which controls the stereoselectivity of multicopper oxidase(VdtB)-catalyzed phenol coupling in viriditoxin biosynthesis
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Fungi: NE > Dikarya: NE > Ascomycota: NE > saccharomyceta: NE > Pezizomycotina: NE > leotiomyceta: NE > Eurotiomycetes: NE > Eurotiomycetidae: NE > Eurotiales: NE > Thermoascaceae: NE > Byssochlamys: NE > Byssochlamys spectabilis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MFMTQIVFGIAPTLLKTFSHLTALDLWRPSAPYVFDPVTSSTYLGTIADG VEEFLGIFYGQDTGGSNRFAPPKPYIPSRHSFINASTAGAACPQPYVPLP ADPYTVLTNVSEDCLSLRIARPENTKSTAKLPVMVWLYGGGASVGTAYDV SYNPVGLIQQSVVNGSPVIYVAINYRVNLFGHAFSDALLKSKSTNLAMQD QRLGIEWIKNHISAFGGDPDNITLFGEDEGATYIALHILSNHEVPFHRAI LQSGAAITHHDVNGNRSARNFAAVAARCNCLSDGDRQVDSQDTVDCLRRV PMEDLVNATFEVAHSVDPVNGFRAFMPAVDGYMIPDEPSNLLSRGQVPAN ISILAGWTRDESSMSVPTSIRTAADAASFISTQFPLLNASTIHHFLTSLY PESDFTTNSPSSPEKVTPAWRATSALHRDLTLTCPTIFQAWSLRLSSNCT TPVYLYELRQSPFATALNNSGVGYLGIVHFSDVPYVFNELERTYYITDPE ENKLAQRMSASWTAFASGAFPLCERSERSLGRWEEAYGGDRVCRDRMPEH VRVKGIGDNGDQDDGDEIGKLMARCGFINRLEY
Reference
Title: Fungal Dirigent Protein Controls the Stereoselectivity of Multicopper Oxidase-Catalyzed Phenol Coupling in Viriditoxin Biosynthesis Hu J, Li H, Chooi YH Ref: Journal of the American Chemical Society, 141:8068, 2019 : PubMed
Paecilomyces variotii produces the antibacterial and cytotoxic ( M)-viriditoxin (1) together with a trace amount of its atropisomer ( P)-viriditoxin 1'. Elucidation of the biosynthesis by heterologous pathway reconstruction in Aspergillus nidulans identified the multicopper oxidase (MCO) VdtB responsible for the regioselective 6,6'-coupling of semiviriditoxin (10), which yielded 1 and 1' at a ratio of 1:2. We further uncovered that VdtD, an alpha/beta hydrolase-like protein lacking the catalytic serine, directs the axial chirality of the products. Using recombinant VdtB and VdtD as cell-free extracts from A. nidulans, we demonstrated that VdtD acts like a dirigent protein to control the stereoselectivity of the coupling catalyzed by VdtB to yield 1 and 1' at a ratio of 20:1. Furthermore, we uncovered a unique Baeyer-Villiger monooxygenase (BVMO) VdtE that could transform the alkyl methylketone side chain to methyl ester against the migratory aptitude.
