Research Topics
Genomes and GenesSpecies | D B JanssenSummaryAffiliation: University of Groningen Country: The Netherlands Publications
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Detail Information
Publications
Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a rhodococcus haloalkane dehalogenaseTjibbe Bosma
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochemistry 42:8047-53. 2003..However, whereas in DhlA the rate of halide release represents the slowest step in the catalytic cycle, our results suggest that in DhaA the release of 3-bromo-1-propanol is the slowest step during 1,3-dibromopropane conversion...- Synthesis of enantiopure chloroalcohols by enzymatic kinetic resolutionRobert M Haak
Department of Organic and Molecular Inorganic Chemistry, Stratingh Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Org Biomol Chem 5:318-23. 2007..Yields were close to the theoretical maximum for all substrates employed. Furthermore, the applicability of this methodology on multigram scale has been established... 
Biodegradation kinetics of 4-fluorocinnamic acid by a consortium of Arthrobacter and Ralstonia strainsSyed A Hasan
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, Groningen, The Netherlands
Biodegradation 23:117-25. 2012....- 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 Microbiol Biotechnol 78:709-17. 2008..These results indicate that the biodegradation of 4-FP starts with a 4-FP monooxygenase reaction that yields benzoquinone, which is reduced to hydroquinone and further metabolized via the beta-ketoadipic acid pathway... - Enantioselective formation and ring-opening of epoxides catalysed by halohydrin dehalogenasesD B Janssen
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, Groningen, The Netherlands
Biochem Soc Trans 34:291-5. 2006.... - Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activitiesDick B Janssen
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Environ Microbiol 7:1868-82. 2005.... - Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate rangeJ P Schanstra
Laboratory of Biochemistry, BIOSON Research Institute, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Biochemistry 35:13186-95. 1996..It is proposed that Phe172 is involved in stabilization of the helix-loop-helix structure that covers the active site of the enzyme and creates a rigid hydrophobic cavity for small apolar halogenated alkanes... - Repositioning the catalytic triad aspartic acid of haloalkane dehalogenase: effects on stability, kinetics, and structureG H Krooshof
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochemistry 36:9571-80. 1997.... - Kinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding siteG H Krooshof
Laboratory of Biochemistry, BIOSON Research Institute, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Biochemistry 37:15013-23. 1998..These structural changes indicate a weakened interaction between residue 175 and the halogen atom or halide ion in the active site and help to explain the kinetic changes induced by the Trp175Tyr mutation... - Kinetics of halide release of haloalkane dehalogenase: evidence for a slow conformational changeJ P Schanstra
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Biochemistry 35:5624-32. 1996..2H2O mainly affected the rate of the conformational change, which is in agreement with this step being rate-limiting and the overall stabilizing effect of 2H2O on the conformation of proteins... - Specificity and kinetics of haloalkane dehalogenaseJ P Schanstra
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Biol Chem 271:14747-53. 1996..The study provides a basis for the analysis of rate-determining steps in the hydrolysis of various environmentally important substrates... - Roles of horizontal gene transfer and gene integration in evolution of 1,3-dichloropropene- and 1,2-dibromoethane-degradative pathwaysG J Poelarends
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands
J Bacteriol 182:2191-9. 2000..The data indicate that horizontal gene transfer and integrase-dependent gene acquisition were the key mechanisms for the evolution of catabolic pathways for the man-made chemicals 1, 3-dichloropropene and 1,2-dibromoethane... - Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studiesW B Alkema
Department of Biochemistry, BIOSON Research Institute, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Protein Eng 13:857-63. 2000..The combined results of the structural and kinetic studies show the importance of alphaF146 in the beta-lactam binding site and provide leads for engineering mutants with improved synthetic properties... - Highly enantioselective and regioselective biocatalytic azidolysis of aromatic epoxidesJ H Spelberg
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, and Department of Organic and Molecular Inorganic Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Org Lett 3:41-3. 2001..In a large scale conversion, the decrease in yield and selectivity due to the uncatalyzed chemical side reaction could be overcome by slow addition of azide... - Degradation of 1,2-dibromoethane by Mycobacterium sp. strain GP1G J Poelarends
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands
J Bacteriol 181:2050-8. 1999..rhodochrous NCIMB 13064, was fused to a fragment of a haloalcohol dehalogenase gene that was identical to the last 42 nucleotides of the hheB gene found in Corynebacterium sp. strain N-1074... - 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... - 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... - Effects of iron limitation on the degradation of toluene by Pseudomonas strains carrying the tol (pWWO) plasmidI J Dinkla
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 67:3406-12. 2001..Growth yields were reduced and substrate affinities decreased under iron-limited conditions, suggesting that iron availability can be an important parameter in the oxidative breakdown of hydrocarbons... - trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomeraseG J Poelarends
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands
J Bacteriol 183:4269-77. 2001..Based on these findings, a novel dehalogenation mechanism is proposed for the CaaD-catalyzed reaction which does not involve the formation of a covalent enzyme-substrate intermediate... - Influence of mutations of Val226 on the catalytic rate of haloalkane dehalogenaseJ P Schanstra
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Protein Eng 10:53-61. 1997..These studies indicate that wild-type haloalkane dehalogenase is optimized for 1,2-dichloroethane, although 1,2-dibromoethane is a better substrate... - Microbial dehalogenationD B Janssen
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, NL 9747 AG, Groningen, The Netherlands
Curr Opin Biotechnol 12:254-8. 2001..Sequence analysis and mutagenesis studies indicate that several dehalogenases are homologous to enzymes that carry out transformations on non-halogenated substrates... - Trichloroethene degradation in a two-step system by methylosinus trichosporium OB3b. Optimization of system performance: use of formate and methaneE M Sipkema
Department of Chemical Engineering, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biotechnol Bioeng 63:56-68. 1999..The model provides a tool for the design of an effective and low-cost treatment system based on methane addition in the conversion reactor... - Effect of mass transfer limitations on the enzymatic kinetic resolution of epoxides in a two-liquid-phase systemH Baldascini
Department of Chemical Engineering, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Biotechnol Bioeng 73:44-54. 2001..Resolution of a 39 g/L solution of racemic styrene oxide in octane was successfully carried out in an emulsion batch reactor to obtain (S)-styrene oxide in high enantiomeric excess (>95% e.e.) with a yield of 30%... - Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding siteR M de Jong
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen, The Netherlands
EMBO J 22:4933-44. 2003..Structure-based sequence analysis reveals that the various haloalcohol dehalogenases have likely originated from at least two different NAD-binding SDR precursors... - Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB geneJ van der Ploeg
Department of Biochemistry, Groningen Biotechnology Center, University of Groningen, The Netherlands
J Bacteriol 173:7925-33. 1991..5 and 61.0% similarity) with the two other haloacid dehalogenases sequenced to date but not with the haloalkane dehalogenase from X. autotrophicus GJ10... - Simultaneous growth on citrate reduces the effects of iron limitation during toluene degradation in PseudomonasI J T Dinkla
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Microb Ecol 45:97-107. 2003..The results indicate that the availability of low concentrations of natural organic compounds, such as produced in the rhizosphere, may positively influence the degradative performance of hydrocarbon-degrading bacteria... - Biocatalysis by dehalogenating enzymesDick B Janssen
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Adv Appl Microbiol 61:233-52. 2007 - Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase geneTjibbe Bosma
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 68:3582-7. 2002.... - Generating segmental mutations in haloalkane dehalogenase: a novel part in the directed evolution toolboxMariel G Pikkemaat
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands
Nucleic Acids Res 30:E35-5. 2002..The results show that the mutagenesis method presented here is an effective tool for accessing formerly unexplorable sequence space and can contribute to the success of future directed evolution experiments... - Complete biodegradation of 4-fluorocinnamic acid by a consortium comprising Arthrobacter sp. strain G1 and Ralstonia sp. strain H1Syed A Hasan
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands
Appl Environ Microbiol 77:572-9. 2011..Degradation of 4-fluorobenzoic acid by strain H1 proceeded via 4-fluorocatechol, which was converted by an ortho-cleavage pathway... - 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... - The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase familyRené M de Jong
Laboratory of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Bacteriol 188:4051-6. 2006..These results broaden the insight into the structural determinants that govern reactivity and selectivity in the haloalcohol dehalogenase family... - Sequential kinetic resolution catalyzed by halohydrin dehalogenaseMaja Majeric Elenkov
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Org Lett 8:4227-9. 2006..8% ee (40% yield) and (S)-2 with 95.2% ee (41% yield). This reaction is carried out in aqueous solution under mild conditions and provides access to a useful statin side-chain building block... - 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... - Molecular dynamics simulations as a tool for improving protein stabilityMariel G Pikkemaat
Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747AG, The Netherlands
Protein Eng 15:185-92. 2002..The results show that MD simulations are capable of identifying mobile protein domains that can successfully be used as a target for stability enhancement by the introduction of a disulfide cross-link... - 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... - 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... - Crystallization and preliminary X-ray analysis of an enantioselective halohydrin dehalogenase from Agrobacterium radiobacter AD1René M de Jong
Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Acta Crystallogr D Biol Crystallogr 58:176-8. 2002..5, c = 121.4 A, and contain two monomers in the asymmetric unit. The crystals diffract to 3.0 A resolution with X-rays from a Cu Kalpha rotating-anode generator... - Catalytic promiscuity of halohydrin dehalogenase and its application in enantioselective epoxide ring openingGhannia Hasnaoui-Dijoux
Groningen Biomolecular Science and Biotechnology Institute, University of Groningen, Groningen, The Netherlands
Chembiochem 9:1048-51. 2008 - 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.... 
One pot 'click' reactions: tandem enantioselective biocatalytic epoxide ring opening and [3+2] azide alkyne cycloadditionLachlan S Campbell-Verduyn
Stratingh Institute for Chemistry, University of Groningen, Groningen, The Netherlands
Chem Commun (Camb) 46:898-900. 2010....- Diversity and biocatalytic potential of epoxide hydrolases identified by genome analysisBert van Loo
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Appl Environ Microbiol 72:2905-17. 2006..The results show that the expression of epoxide hydrolase genes that are detected by analyses of genomic databases is a useful strategy for obtaining new biocatalysts... - Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by halo alcohol dehalogenase HheCRené M de Jong
Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, NL 9747 AG Groningen, The Netherlands
J Am Chem Soc 127:13338-43. 2005..This work represents a rare opportunity to explain the enantioselectivity of an enzymatic reaction by comparison of crystallographic data on the binding of both the favored and unfavored enantiomers... - 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.... - Evolving haloalkane dehalogenasesDick B Janssen
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Curr Opin Chem Biol 8:150-9. 2004..To improve enzymatic degradation of some environmentally important recalcitrant compounds, site-directed mutagenesis and directed-evolution studies are being done... - Biocatalytic conversion of epoxidesErik J de Vries
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands
Curr Opin Biotechnol 14:414-20. 2003..The emerging new possibilities for enantioselective biocatalytic conversion of epoxides suggests that their importance in green chemistry will grow... - Quantifying the accessibility of the metagenome by random expression cloning techniquesEsther M Gabor
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Environ Microbiol 6:879-86. 2004..Our study reveals significant differences in the predicted expression modes between distinct taxonomic groups of organisms and suggests that about 40% of the enzymatic activities may be readily recovered by random cloning in E. coli... - 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... - 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... - Formation of enantiopure 5-substituted oxazolidinones through enzyme-catalysed kinetic resolution of epoxidesMaja Majerić Elenkov
Ruder Boskovic Institute, Zagreb, Croatia
Org Lett 10:2417-20. 2008..This is the first example of the biocatalytic conversion of a range of epoxides to the corresponding oxazolidinones... - Inactivation of epoxide hydrolase by catalysis-induced formation of isoaspartateBert van Loo
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
FEBS Lett 582:1581-6. 2008..Inactivation occurred at a lower rate with the (S)-enantiomer of para-nitrostyrene epoxide, indicating that it is related to the structure of the covalent hydroxyalkyl-enzyme intermediate... - Kinetics of enzyme acylation and deacylation in the penicillin acylase-catalyzed synthesis of beta-lactam antibioticsWynand B L Alkema
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Eur J Biochem 270:3675-83. 2003..By combining the results of the steady-state, presteady state and nucleophile binding experiments, values for the relevant kinetic constants for the synthesis and hydrolysis of beta-lactam antibiotics were obtained... - Catalytic mechanism of the maloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26Zbynek Prokop
National Centre for Biomolecular Research, Masaryk University, Kotlarska 2, 611 37 Brno, Czech Republic
J Biol Chem 278:45094-100. 2003.... - 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... - Role of alphaArg145 and betaArg263 in the active site of penicillin acylase of Escherichia coliWynand B L Alkema
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Biochem J 365:303-9. 2002.... - 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... - 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... - Identification of the catalytic residues of alpha-amino acid ester hydrolase from Acetobacter turbidans by labeling and site-directed mutagenesisJolanda J Polderman-Tijmes
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen, The Netherlands
J Biol Chem 277:28474-82. 2002..This distinguishes the alpha-amino acid ester hydrolase from the Ntn-hydrolase family of beta-lactam antibiotic acylases... - Directed evolution of epoxide hydrolase from A. radiobacter toward higher enantioselectivity by error-prone PCR and DNA shufflingBert van Loo
Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Chem Biol 11:981-90. 2004..Several mutations in the shuffled mutants had additive effects... - Degradation of fluorobenzene by Rhizobiales strain F11 via ortho cleavage of 4-fluorocatechol and catecholMaria F Carvalho
Escola Superior de Biotecnologia, , , 4200-072 Porto, Portugal
Appl Environ Microbiol 72:7413-7. 2006..The results suggest that fluorobenzene is predominantly degraded via 4-fluorocatechol with subsequent ortho cleavage and also partially via catechol... - Increasing the synthetic performance of penicillin acylase PAS2 by structure-inspired semi-random mutagenesisEsther M Gabor
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
Protein Eng Des Sel 17:571-9. 2004..Although catalytic activity dropped by a factor of 5-10, the enhanced synthetic performance of the recovered penicillin acylase variants makes them interesting biocatalysts for the production of beta-lactam antibiotics... - 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... - The role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylaseWynand B L Alkema
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, The Netherlands
Eur J Biochem 269:2093-100. 2002..The reduced specificity for the product and the high initial transferase/hydrolase ratio of betaF24A resulted in high yields in acyl transfer reactions... - Acetobacter turbidans alpha-amino acid ester hydrolase: how a single mutation improves an antibiotic-producing enzymeThomas R M Barends
Laboratories of Biophysical Chemistry and Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
J Biol Chem 281:5804-10. 2006..Because this changes the properties of the beta-lactam binding site, this could explain the increased beta-lactam transferase activity of this mutant... - Metabolism of mono- and dihalogenated C1 and C2 compounds by Xanthobacter autotrophicus growing on 1,2-dichloroethaneMaciej Torz
Institute of Chemical Engineering, Bulgarian Academy of Sciences, Acad G Bonchev Str, Bl 103, 113, Sofia, Bulgaria
Biodegradation 18:145-57. 2007..Our results extend the spectrum of halogenated C1 and C2 compounds that are known to be degraded by strain GJ10 and provide information on toxic effects and transformation of compounds not serving as a carbon source for this bacterium...