Research Topics
| Susanne FetznerSummaryCountry: Germany Publications
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Detail Information
Publications
Ring-cleaving dioxygenases with a cupin foldSusanne Fetzner
Institute of Molecular Microbiology and Biotechnology, Westfalian Wilhelms University Munster, Munster, Germany
Appl Environ Microbiol 78:2505-14. 2012..The tentative hypothesis that quercetinase catalysis involves direct electron transfer from metal-bound flavonolate to O(2) is supported by model chemistry...
Cofactor-independent oxidases and oxygenasesSusanne Fetzner
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, Munster, Germany
Appl Microbiol Biotechnol 86:791-804. 2010..Nevertheless, they all may share the common mechanistic concept of initial base-catalyzed activation of their organic substrate and "substrate-assisted catalysis"...
Quercetinase QueD of Streptomyces sp. FLA, a monocupin dioxygenase with a preference for nickel and cobaltHedda Merkens
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, 48149 Munster, Germany
Biochemistry 47:12185-96. 2008..On the basis of spectroscopic data, and considering the organic chemistry of flavonols, a nonredox role of the metal center in catalysis is discussed...
Transcriptional analysis of the queD gene coding for quercetinase of Streptomyces sp. FLAHedda Merkens
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, Munster, Germany
FEMS Microbiol Lett 287:100-7. 2008..Sequence analysis of the queD promoter region indicated possible binding sites for an LmrA/YxaF-like repressor...
Complete nucleotide sequence of the 113-kilobase linear catabolic plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61a and transcriptional analysis of genes involved in quinaldine degradationKatja Parschat
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, D 48149 Munster, Germany
J Bacteriol 189:3855-67. 2007..Even if the putative proteins encoded by ORFs 101 to 103 share motifs with the Tap and terminal proteins involved in telomere patching of Streptomyces linear replicons, their overall sequences and domain structures differ significantly...
A novel replicative enzyme encoded by the linear Arthrobacter plasmid pAL1Stephan Kolkenbrock
Institute of Molecular Microbiology and Biotechnology, Westfalian Wilhelms University Munster, Corrensstrasse 3, D 48149 Munster, Germany
J Bacteriol 192:4935-43. 2010..Enzyme assays suggested that the protein exhibits DNA topoisomerase, DNA helicase, and DNA- and protein-primed DNA polymerase activities. The pAL1.101 protein, therefore, may act as a replicase of pAL1...
A new monocupin quercetinase of Streptomyces sp. FLA: identification and heterologous expression of the queD gene and activity of the recombinant enzyme towards different flavonolsHedda Merkens
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, Corrensstr 3, 48149 Munster, Germany
Arch Microbiol 187:475-87. 2007..This arrangement suggests that queD is not part of a catabolic gene cluster. Quercetinases might play a major role as detoxifying rather than catabolic enzymes...
EstA from Arthrobacter nitroguajacolicus Rü61a, a thermo- and solvent-tolerant carboxylesterase related to class C beta-lactamasesMarcus Schütte
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, Corrensstrasse 3, D 48149, Munster
Curr Microbiol 54:230-6. 2007....
Identification and in vitro deoxynucleotidylation of the terminal protein of the linear plasmid pAL1 of Arthrobacter nitroguajacolicus Rü61aStephan Kolkenbrock
Institute of Molecular Microbiology and Biotechnology, University of Munster, Munster, Germany
FEMS Microbiol Lett 304:169-76. 2010..Consistent with its proposed role as a protein primer in DNA synthesis, pORF102 was deoxynucleotidylated in vitro with dCMP, complementary to the 3'-ends (... GCAGG) of pAL1...
Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanismKristian Boehm
Institut fur Physikalische Chemie, Westfalische Wilhelms Universitat Munster, Corrensstrasse 30, 48149 Munster, Germany
Biochemistry 47:7116-26. 2008..This was the case for the CD-monitored urea unfolding curve...
Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilateJörg Overhage
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, Corrensstrasse 3, D 48149 Munster, Germany
Microbiology 151:491-500. 2005..A 478 bp fragment that on pAL1 represents an intergenic region showed 100 % sequence identity in all isolates harbouring a pAL1-like plasmid, suggesting horizontal dissemination of the linear plasmid among the genus Arthrobacter...
Synthesis and biotransformation of 2-alkyl-4(1H)-quinolones by recombinant Pseudomonas putida KT2440Heiko Niewerth
Institute of Molecular Microbiology and Biotechnology, University of Munster, 48149 Munster, Germany
Appl Microbiol Biotechnol 91:1399-408. 2011..putida KT2440 [pBBR-pqsH]. PQS can be isolated from methanolic cell extracts by HPLC, or be precipitated as Fe(III)-PQS complex. Preparation of a library of AQs will facilitate studies on the biological functions of these compounds...
Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation ofUrsula Frerichs-Deeken
Institut fur Molekulare Mikrobiologie und Biotechnologie, Westfalische Wilhelms Universitat Munster, D 48149 Munster, Germany
Biochemistry 43:14485-99. 2004..Subsequent intramolecular attack would result in the 2,4-endoperoxy (di)anion that may collapse to the reaction products...
Dioxygenases without requirement for cofactors: identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenaseUrsula Frerichs-Deeken
, , , Germany
Curr Microbiol 51:344-52. 2005....
