The flavin monooxygenases

S. Montersino, W.J.H. van Berkel

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

4 Citations (Scopus)

Abstract

Flavin monooxygenases are ubiquitous enzymes that catalyze a wide variety of regio -and enantioselective oxygenation reactions via the formation of a fl avin C4a-(hydro)peroxide intermediate. Based on fold and function, fl avin monooxygenases can be divided into six subfamilies. Subclasses A and B comprise single-component enzymes that rely on NAD(P)H as electron donor. Subclasses C–F comprise two-component enzymes , composed of a fl avin reductase and a fl avin-specifi c monooxygenase . FAD-containing hydroxylases (subclass A ) convert many (hetero)aromatic substrates ranging from monophenols and uric acids to polyketide antibiotics and antitumor agents. FAD-containing monooxygenases (subclass B ) perform Baeyer-Villiger oxidation, sulfoxidation and heteroatom hydroxylation reactions. FMN-dependent TIM-barrel enzymes (subclass C ) catalyze Baeyer-Villiger oxidation, hydroxylation of long-chain alkanes and nitriloacetate, oxidation and desulfurization of sulfonates, and oxidation of aldehydes coupled with generation of bioluminescence. FMN/FAD hydroxylases with an acyl-CoA dehydrogenase fold (subclass D ) convert mono- and polyphenols. FAD-specifi c styrene monooxygenases (subclass E ) oxidize styrene derivatives to the corresponding epoxides. FAD-specifi c halogenases (subclass F ) catalyze the regioselective chlorination and bromination of activated organic molecules for the production of antibiotics, antitumor agents and other natural products. During the past few years, many new family members and several unprecedented fl avin monooxygenase reactions have emerged. This review illustrates selected features, tools to retrieve novel fl avin monooxygenases from genome mining, and new findings on each of the six subclasses.
LanguageEnglish
Title of host publicationHandbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods
EditorsR. Hille, S.M. Miller, B. Palfey
Place of PublicationBerlin
PublisherDe Gruyter
Pages51-72
Number of pages500
ISBN (Print)9783110298284
Publication statusPublished - 2013

Fingerprint

Mixed Function Oxygenases
Flavin-Adenine Dinucleotide
Flavin Mononucleotide
Oxidation
Hydroxylation
Enzymes
Antineoplastic Agents
Acyl-CoA Dehydrogenase
Anti-Bacterial Agents
Bioluminescence
Polyketides
Alkanes
Styrene
Oxygenation
4,6-dinitro-o-cresol
Chlorination
Epoxy Compounds
Peroxides
Polyphenols
Desulfurization

Cite this

Montersino, S., & van Berkel, W. J. H. (2013). The flavin monooxygenases. In R. Hille, S. M. Miller, & B. Palfey (Eds.), Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods (pp. 51-72). Berlin: De Gruyter.
Montersino, S. ; van Berkel, W.J.H. / The flavin monooxygenases. Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods. editor / R. Hille ; S.M. Miller ; B. Palfey. Berlin : De Gruyter, 2013. pp. 51-72
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Montersino, S & van Berkel, WJH 2013, The flavin monooxygenases. in R Hille, SM Miller & B Palfey (eds), Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods. De Gruyter, Berlin, pp. 51-72.

The flavin monooxygenases. / Montersino, S.; van Berkel, W.J.H.

Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods. ed. / R. Hille; S.M. Miller; B. Palfey. Berlin : De Gruyter, 2013. p. 51-72.

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

TY - CHAP

T1 - The flavin monooxygenases

AU - Montersino, S.

AU - van Berkel, W.J.H.

PY - 2013

Y1 - 2013

N2 - Flavin monooxygenases are ubiquitous enzymes that catalyze a wide variety of regio -and enantioselective oxygenation reactions via the formation of a fl avin C4a-(hydro)peroxide intermediate. Based on fold and function, fl avin monooxygenases can be divided into six subfamilies. Subclasses A and B comprise single-component enzymes that rely on NAD(P)H as electron donor. Subclasses C–F comprise two-component enzymes , composed of a fl avin reductase and a fl avin-specifi c monooxygenase . FAD-containing hydroxylases (subclass A ) convert many (hetero)aromatic substrates ranging from monophenols and uric acids to polyketide antibiotics and antitumor agents. FAD-containing monooxygenases (subclass B ) perform Baeyer-Villiger oxidation, sulfoxidation and heteroatom hydroxylation reactions. FMN-dependent TIM-barrel enzymes (subclass C ) catalyze Baeyer-Villiger oxidation, hydroxylation of long-chain alkanes and nitriloacetate, oxidation and desulfurization of sulfonates, and oxidation of aldehydes coupled with generation of bioluminescence. FMN/FAD hydroxylases with an acyl-CoA dehydrogenase fold (subclass D ) convert mono- and polyphenols. FAD-specifi c styrene monooxygenases (subclass E ) oxidize styrene derivatives to the corresponding epoxides. FAD-specifi c halogenases (subclass F ) catalyze the regioselective chlorination and bromination of activated organic molecules for the production of antibiotics, antitumor agents and other natural products. During the past few years, many new family members and several unprecedented fl avin monooxygenase reactions have emerged. This review illustrates selected features, tools to retrieve novel fl avin monooxygenases from genome mining, and new findings on each of the six subclasses.

AB - Flavin monooxygenases are ubiquitous enzymes that catalyze a wide variety of regio -and enantioselective oxygenation reactions via the formation of a fl avin C4a-(hydro)peroxide intermediate. Based on fold and function, fl avin monooxygenases can be divided into six subfamilies. Subclasses A and B comprise single-component enzymes that rely on NAD(P)H as electron donor. Subclasses C–F comprise two-component enzymes , composed of a fl avin reductase and a fl avin-specifi c monooxygenase . FAD-containing hydroxylases (subclass A ) convert many (hetero)aromatic substrates ranging from monophenols and uric acids to polyketide antibiotics and antitumor agents. FAD-containing monooxygenases (subclass B ) perform Baeyer-Villiger oxidation, sulfoxidation and heteroatom hydroxylation reactions. FMN-dependent TIM-barrel enzymes (subclass C ) catalyze Baeyer-Villiger oxidation, hydroxylation of long-chain alkanes and nitriloacetate, oxidation and desulfurization of sulfonates, and oxidation of aldehydes coupled with generation of bioluminescence. FMN/FAD hydroxylases with an acyl-CoA dehydrogenase fold (subclass D ) convert mono- and polyphenols. FAD-specifi c styrene monooxygenases (subclass E ) oxidize styrene derivatives to the corresponding epoxides. FAD-specifi c halogenases (subclass F ) catalyze the regioselective chlorination and bromination of activated organic molecules for the production of antibiotics, antitumor agents and other natural products. During the past few years, many new family members and several unprecedented fl avin monooxygenase reactions have emerged. This review illustrates selected features, tools to retrieve novel fl avin monooxygenases from genome mining, and new findings on each of the six subclasses.

M3 - Chapter

SN - 9783110298284

SP - 51

EP - 72

BT - Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods

A2 - Hille, R.

A2 - Miller, S.M.

A2 - Palfey, B.

PB - De Gruyter

CY - Berlin

ER -

Montersino S, van Berkel WJH. The flavin monooxygenases. In Hille R, Miller SM, Palfey B, editors, Handbook of Flavoproteins Vol. II: Complex Flavoproteins, Dehydrogenases and Physical Methods. Berlin: De Gruyter. 2013. p. 51-72