Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

被引：547

作者：

van Berkel, W. J. H.

Kamerbeek, N. M.

Fraaije, M. W.

机构：

[1] Univ Groningen, Biochem Lab, Groningen Biomol Sci & Biotechnol Inst, NL-9747 AG Groningen, Netherlands

[2] Univ Wageningen, Biochem Lab, Dept Agrotechnol & Food Sci, NL-6703 HA Wageningen, Netherlands

[3] Sanquin Res, Dept Blood Cell Res, NL-1066 CX Amsterdam, Netherlands

来源：

JOURNAL OF BIOTECHNOLOGY | 2006年 / 124卷 / 04期

关键词：

flavoprotein monooxygenase; hydroxylation; sulfoxidation; epoxidation; Baeyer-Villiger oxidation; biocatalysis;

D O I：

10.1016/j.jbiotec.2006.03.044

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

During the last decades a large number of flavin-dependent monooxygenases have been isolated and studied. This has revealed that flavoprotein monooxygenases are able to catalyze a remarkable wide variety of oxidative reactions such as regioselective hydroxylations and enantioselective sulfoxidations. These oxidation reactions are often difficult, if not impossible, to be achieved using chemical approaches. Analysis of the available genome sequences has indicated that many more flavoprotein monooxygenases exist and await biocatalytic exploration. Based on the known biochemical properties of a number of flavoprotein monooxygenases and sequence and structural analyses, flavoprotein monooxygenases can be classified into six distinct flavoprotein monooxygenase subclasses. This review provides an inventory of known flavoprotein monooxygenases belonging to these different enzyme subclasses. Furthermore, the biocatalytic potential of a selected number of flavoprotein monooxygenases is highlighted. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：670 / 689

页数：20

共 140 条

[1] Microbial desulfurization of diesel oils by selected bacterial strains [J].

Abbad-Andaloussi, S ;

Warzywoda, M ;

Monot, F .

OIL & GAS SCIENCE AND TECHNOLOGY-REVUE D IFP ENERGIES NOUVELLES, 2003, 58 (04) :505-513

[2] Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli [J].

Adams, MA ;

Jia, ZC .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (09) :8358-8363

[3] Monooxygenase-like sequence of a Rhodococcus equi gene conferring increased resistance to rifampin by inactivating this antibiotic [J].

Andersen, SJ ;

Quan, S ;

Gowan, B ;

Dabbs, ER .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1997, 41 (01) :218-221

[4]

[Anonymous], MICROBIAL DEGRADATIO

[5] Chemostat approach for the directed evolution of biodesulfurization gain-of-function mutants [J].

Arensdorf, JJ ;

Loomis, AK ;

DiGrazia, PM ;

Monticello, DJ ;

Pienkos, PT .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2002, 68 (02) :691-698

[6] Structure of bacterial luciferase [J].

Baldwin, TO ;

Christopher, JA ;

Raushel, FM ;

Sinclair, JF ;

Ziegler, MM ;

Fisher, AJ ;

Rayment, I .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1995, 5 (06) :798-809

[7] Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: Towards practical Baeyer-Villiger monooxygenases [J].

Bocola, M ;

Schulz, F ;

Leca, F ;

Vogel, A ;

Fraaije, MW ;

Reetz, MT .

ADVANCED SYNTHESIS & CATALYSIS, 2005, 347 (7-8) :979-986

[8] Heterologous expression of the naphthocyclinone hydroxylase gene from Streptomyces arenae for production of novel hybrid polyketides [J].

Brünker, P ;

Sterner, O ;

Bailey, JE ;

Minas, W .

ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY, 2001, 79 (3-4) :235-245

[9] Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants [J].

Bugos, RC ;

Hieber, AD ;

Yamamoto, HY .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (25) :15321-15324

[10] A novel two-protein component flavoprotein hydroxylase -: p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii [J].

Chaiyen, P ;

Suadee, C ;

Wilairat, P .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (21) :5550-5561

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