Research Topics
Genomes and Genes | M W FraaijeSummaryAffiliation: University of Groningen Country: The Netherlands Publications
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Publications
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidaseM W Fraaije
Department of Genetics, University of Pavia, via Abbiategrasso 207, 27100 Pavia, Italy
J Biol Chem 274:35514-20. 1999..Thus, formation of a histidyl-FAD bond in specific flavoenzymes might have evolved as a way to contribute to the enhancement of their oxidative power...- Structural analysis of flavinylation in vanillyl-alcohol oxidaseM W Fraaije
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Biol Chem 275:38654-8. 2000..Furthermore, our studies clearly demonstrate that in VAO, the FAD binds via a typical lock-and-key approach to a preorganized binding site... - Discovery of a thermostable Baeyer-Villiger monooxygenase by genome miningMarco W Fraaije
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Appl Microbiol Biotechnol 66:393-400. 2005..This study demonstrates that, using effective annotation tools, genomes can efficiently be exploited as a source of novel BVMOs... - Identification of a Baeyer-Villiger monooxygenase sequence motifMarco W Fraaije
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
FEBS Lett 518:43-7. 2002..Using these novel amino acid sequence fingerprints, BVMOs and FMOs can be readily identified in the protein sequence databank... - Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificityA Mattevi
Department of Genetics and Microbiology, University of Pavia, Italy
Structure 5:907-20. 1997.... - 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compoundsN M Kamerbeek
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Eur J Biochem 268:2547-57. 2001..From a kinetic analysis of the G490A mutant it is concluded that the observed sequence motif serves a structural function which is of importance for NADPH binding... - Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimumA Mattevi
Department of Genetics and Microbiology, University of Pavia, Italy
Proteins 27:601-3. 1997..5 A, c = 132.9 A. Diffraction data have been recorded to 3.2 A resolution by using a laboratory source and to 2.5 A resolution on flash freezing the crystal at the ELETTRA Synchrotron X-ray diffraction beam line... - A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamilyEdwin van Bloois
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, The Netherlands
Appl Microbiol Biotechnol 86:1419-30. 2010..In conclusion, the detailed biochemical characterization reported here contributes significantly to our understanding of these enzymes and further emphasizes their biotechnological potential... - The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenaseMarco W Fraaije
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Biol Chem 279:3354-60. 2004..This reactivity and substrate acceptance-profiling study provides valuable information concerning this newly identified prodrug activator from M. tuberculosis... - Enzymatic synthesis of vanillinR H van den Heuvel
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Agric Food Chem 49:2954-8. 2001..This route to vanillin has biotechnological potential as the widely available principle of red pepper, capsaicin, can be hydrolyzed enzymatically to vanillylamine... - Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/reductasesJ E van Hylckama Vlieg
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, NL-9747 AG Groningen, The Netherlands
J Bacteriol 183:5058-66. 2001..The proposed mechanism is fundamentally different from that of the well-studied hydrolytic dehalogenases, since it does not involve a covalent enzyme-substrate intermediate... - Substrate specificity and enantioselectivity of 4-hydroxyacetophenone monooxygenaseNanne M Kamerbeek
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 69:419-26. 2003..The biocatalytic properties of HAPMO described here show the potential of this enzyme for biotechnological applications... - Hydroquinone dioxygenase from pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenasesMariëlle J H Moonen
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Bacteriol 190:5199-209. 2008..HQDO is a novel member of the family of nonheme-iron(II)-dependent dioxygenases. The enzyme shows insignificant sequence identity with known dioxygenases... - Flavoprotein monooxygenases, a diverse class of oxidative biocatalystsW J H van Berkel
Laboratory of Biochemistry, Department of Agrotechnology and Food Sciences, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Biotechnol 124:670-89. 2006..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... - Discovery of a novel styrene monooxygenase originating from the metagenomeErik W van Hellemond
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 73:5832-9. 2007..This excellent enantioselectivity in combination with the moderate sequence identity forms a clear indication that SmoA from a metagenomic origin represents a new enzyme within the small family of styrene monooxygenases... - Kinetic mechanism and enantioselectivity of halohydrin dehalogenase from Agrobacterium radiobacterLixia Tang
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, NL-9747 AG, Groningen, The Netherlands
Biochemistry 42:5378-86. 2003..The high enantiopreference for the (R)-enantiomer can be explained by weak substrate binding of the (S)-enantiomer and a lower rate of reaction at the active site... - Discovery and characterization of a putrescine oxidase from Rhodococcus erythropolis NCIMB 11540Erik W van Hellemond
Laboratory of Biochemistry, University of Groningen, Groningen Biomolecular Sciences and Biotechnology Institute, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Appl Microbiol Biotechnol 78:455-63. 2008..Mutation of this residue resulted in a drastic drop (five orders of magnitude) in catalytic efficiency. Interestingly, the mutant enzyme showed activity with monoamines, which are not accepted by wt-PuORh... - Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applicationsD E Torres Pazmiño
Laboratory of Biochemistry, Dept of Biochemistry, Biotechnology Group, University of Groningen, 9747 AG, Groningen, The Netherlands
J Biotechnol 146:9-24. 2010..This latter overview is of relevance for the biotechnological applications of these oxidative enzymes... - Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidaseFederico Forneris
Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy
Biochemistry 47:978-85. 2008..These features combined with the tight shape of the catalytic site provide insights into the mechanism of AldO-mediated regioselective oxidation reactions and its substrate specificity... - The growing VAO flavoprotein familyNicole G H Leferink
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
Arch Biochem Biophys 474:292-301. 2008..Some VAO-type aldonolactone oxidoreductases favor the non-covalent binding of the flavin cofactor. These enzymes act as dehydrogenases, using cytochrome c as electron acceptor... - Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fuscaDaniel E Torres Pazmiño
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochemistry 47:4082-93. 2008..The mutants were unable to convert either phenylacetone or benzyl methyl sulfide. This demonstrates that R337 is crucially involved in assisting PAMO-mediated Baeyer-Villiger and sulfoxidation reactions... - Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolorDominic P H M Heuts
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Biol Chem 282:20283-91. 2007..Reduced AldO readily reacts with molecular oxygen (1.7 x 10(5) m(-1) s(-1)), which confirms that the enzyme represents a true flavoprotein oxidase... - Discovery of a eugenol oxidase from Rhodococcus sp. strain RHA1Jianfeng Jin
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
FEBS J 274:2311-21. 2007..The ability to efficiently convert eugenol may facilitate biotechnological valorization of this natural aromatic compound... - Steady-state kinetics and tryptophan fluorescence properties of halohydrin dehalogenase from Agrobacterium radiobacter. Roles of W139 and W249 in the active site and halide-induced conformational changeLixia Tang
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochemistry 42:14057-65. 2003.... - Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysisEdwin van Bloois
Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Appl Microbiol Biotechnol 83:679-87. 2009..It is anticipated that these whole-cell systems will be a valuable tool for further biological and industrial exploitation of AldO and other cofactor-containing enzymes... - Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenaseAndrea Alfieri
Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy
Proc Natl Acad Sci U S A 105:6572-7. 2008..Localization of mutations in human FMO3 that are known to cause trimethylaminuria (fish-odor syndrome) in the elucidated FMO structure provides a structural explanation for their biological effects... - Analysis of two gene clusters involved in the degradation of 4-fluorophenol by Arthrobacter sp. strain IF1Maria Isabel M Ferreira
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, NL 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 75:7767-73. 2009.... - Crystal structure of a Baeyer-Villiger monooxygenaseEnrico Malito
Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy
Proc Natl Acad Sci U S A 101:13157-62. 2004.... - Improved catalytic properties of halohydrin dehalogenase by modification of the halide-binding siteLixia Tang
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Biochemistry 44:6609-18. 2005..Taken together, these results show that the disruption of two hydrogen bonds around the halide-binding site increases the rate of halide release and can enhance the overall catalytic activity of HheC... - Baeyer-Villiger monooxygenases: recent advances and future challengesDaniel E Torres Pazmiño
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Curr Opin Chem Biol 14:138-44. 2010..This review provides an overview on the recently gained knowledge on BVMOs and sketches the outlook for future industrial applications of these unique oxidative biocatalysts... - Changing the substrate specificity of a chitooligosaccharide oxidase from Fusarium graminearum by model-inspired site-directed mutagenesisDominic P H M Heuts
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
FEBS Lett 581:4905-9. 2007..The substrate specificity of wild type ChitO and the Q268R mutant were examined and confirmed that Q268 is indeed involved in N-acetyl recognition... - ADP competes with FAD binding in putrescine oxidaseErik W van Hellemond
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Biol Chem 283:28259-64. 2008.... - What's in a covalent bond? On the role and formation of covalently bound flavin cofactorsDominic P H M Heuts
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
FEBS J 276:3405-27. 2009..This review presents an overview of the known types of covalent flavin bonds and the proposed mechanisms and roles of covalent flavinylation... - Redox properties of vanillyl-alcohol oxidaseRobert H H van den Heuvel
Department of Microbiology and Genetics, University of Pavia, 27100 Pavia, Italy
Methods Enzymol 353:177-86. 2002 - Identification of a gatekeeper residue that prevents dehydrogenases from acting as oxidasesNicole G H Leferink
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Biol Chem 284:4392-7. 2009..The presence of such an oxygen access gate seems to be a key factor for the prevention of oxidase activity within the VAO family and is absent in members that act as oxidases... - Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic processJianfeng Jin
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
FEBS J 275:5191-200. 2008..Tandem ESI-MS experiments revealed that octamerization is not dependent on full covalent flavinylation... - Elucidation of the 4-hydroxyacetophenone catabolic pathway in Pseudomonas fluorescens ACBMariëlle J H Moonen
Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
J Bacteriol 190:5190-8. 2008..Based on these findings and additional biochemical evidence, it is proposed that the hapC and hapD gene products are involved in the ring cleavage of hydroquinone... - The role of double covalent flavin binding in chito-oligosaccharide oxidase from Fusarium graminearumDominic P H M Heuts
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochem J 413:175-83. 2008..Besides tuning the redox properties, the bi-covalent binding of the FAD cofactor in ChitO is essential for a catalytically competent conformation of the active site... - Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenasesNanne M Kamerbeek
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Eur J Biochem 271:2107-16. 2004..These results indicate that the strict NADPH dependency of this class of monooxygenases is based upon recognition of the coenzyme by several basic residues... - A highly specific mechanism of histone H3-K4 recognition by histone demethylase LSD1Federico Forneris
Dipartimento di Genetica e Microbiologia, Universita di Pavia, Via Ferrata 1, 27100 Pavia, Italy
J Biol Chem 281:35289-95. 2006..We suggest that after H3-K4 demethylation, LSD1 recruits the forthcoming chromatin remodelers leading to the introduction of gene repression marks... - Joint functions of protein residues and NADP(H) in oxygen activation by flavin-containing monooxygenaseRoberto Orru
Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy
J Biol Chem 285:35021-8. 2010..The necessity of fine tuning the hydrogen-bonding, electrostatics, and accessibility of the flavin will represent a challenge for the design and development of oxidases and monoxygenases for biotechnological applications... - Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenaseRobert H H van den Heuvel
Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University
J Biol Chem 280:32115-21. 2005..The interaction with the coenzyme analog 3-aminopyridine adenine dinucleotide phosphate (AADP(+)) strongly enhanced the thermal stability of wild type HAPMO. This coenzyme-induced stabilization may also be important for related enzymes...