Premium
1‐Hydroxy monocyclic carotenoid 3,4‐dehydrogenase from a marine bacterium that produces myxol
Author(s) -
Teramoto Maki,
Rählert Nina,
Misawa Norihiko,
Sandmann Gerhard
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.05.085
Subject(s) - carotenoid , escherichia coli , biochemistry , enzyme , biosynthesis , gene cluster , bacteria , biology , chemistry , gene , stereochemistry , microbiology and biotechnology , genetics
A crtD (1‐HO carotenoid 3,4‐dehydrogenase gene) homolog from marine bacterium strain P99‐3 included in the gene cluster for the biosynthesis of myxol (3 ′ ,4 ′ ‐didehydro‐1 ′ ,2 ′ ‐dihydro‐β,ψ‐carotene‐3,1 ′ ,2 ′ ‐triol) was functionally identified. The P99‐3 CrtD was phylogenetically distant from the other CrtDs. A catalytic feature was its high activity for the monocyclic carotenoid conversion: 1 ′ ‐HO‐torulene (3 ′ ,4 ′ ‐didehydro‐1 ′ ,2 ′ ‐dihydro‐β,ψ‐caroten‐1 ′ ‐ol) was prominently formed from 1 ′ ‐HO‐γ‐carotene (1 ′ ,2 ′ ‐dihydro‐β,ψ‐caroten‐1 ′ ‐ol) in Escherichia coli with P99‐3 CrtD, indicating that this enzyme has been highly adapted to myxol biosynthesis. This unique type of crtD is a valuable tool for obtaining 1 ′ ‐HO‐3 ′ ,4 ′ ‐didehydro monocyclic carotenoids in a heterologous carotenoid production system.