TY - JOUR
T1 - Two-component fad-dependent monooxygenases
T2 - Current knowledge and biotechnological opportunities
AU - Heine, Thomas
AU - van Berkel, Willem J.H.
AU - Gassner, George
AU - van Pée, Karl Heinz
AU - Tischler, Dirk
PY - 2018/8/2
Y1 - 2018/8/2
N2 - Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single-or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aromatic compounds, and biosynthesis of secondary metabolites. The monooxygenase component of these enzymes is strictly dependent on reduced FAD, which is supplied by the reductase component. More and more representatives of two-component FAD-dependent monooxygenases have been discovered and characterized in recent years, which has resulted in the identification of novel physiological roles, functional properties, and a variety of biocatalytic opportunities.
AB - Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single-or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aromatic compounds, and biosynthesis of secondary metabolites. The monooxygenase component of these enzymes is strictly dependent on reduced FAD, which is supplied by the reductase component. More and more representatives of two-component FAD-dependent monooxygenases have been discovered and characterized in recent years, which has resulted in the identification of novel physiological roles, functional properties, and a variety of biocatalytic opportunities.
KW - Biocatalysis
KW - Epoxidation
KW - Flavin reductase
KW - Flavoprotein monooxygenases
KW - Halogenation
KW - Heteroatom oxidation
KW - Hydroxylation
U2 - 10.3390/biology7030042
DO - 10.3390/biology7030042
M3 - Article
AN - SCOPUS:85055559700
SN - 2079-7737
VL - 7
JO - Biology
JF - Biology
IS - 3
M1 - 42
ER -