Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Edwin van Bloois"'
Publikováno v:
Journal of Industrial Microbiology & Biotechnology, 41(1), 1-7. SPRINGER
DyP peroxidases comprise a novel superfamily of heme-containing peroxidases, which is unrelated to the superfamilies of plant and animal peroxidases. These enzymes have so far been identified in the genomes of fungi, bacteria, as well as archaea, alt
Publikováno v:
Journal of Biomolecular Screening
Journal of Biomolecular Screening, 18(6), 678-687
Journal of Biomolecular Screening, 18(6), 678-687
Baeyer-Villiger monooxygenases (BVMOs) have been receiving increasing attention as enzymes useful for biocatalytic applications. Industrial requirements call for rapid and extensive redesign of these enzymes. In response to the need for screening lar
Autor:
Edwin van Bloois, Marco W. Fraaije, Egon M. A. Rijpkema, Hein J. Wijma, Dominic P. H. M. Heuts, Remko T. Winter
Publikováno v:
Applied Microbiology and Biotechnology, 95(2), 389-403. SPRINGER
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology
We describe the discovery, isolation and characterization of a highly thermostable alditol oxidase from Acidothermus cellulolyticus 11B. This protein was identified by searching the genomes of known thermophiles for enzymes homologous to Streptomyces
Publikováno v:
Trends in Biotechnology. 29:79-86
Bacterial surface display entails the presentation of recombinant proteins or peptides on the surface of bacterial cells. Escherichia coli is the most frequently used bacterial host for surface display and, as such, a variety of E. coli display syste
Publikováno v:
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology, 86(5), 1419-1430. SPRINGER
Applied Microbiology and Biotechnology, 86(5), 1419-1430. SPRINGER
DyP-type peroxidases comprise a novel superfamily of heme-containing peroxidases which is unrelated to the superfamilies of known peroxidases and of which only a few members have been characterized in some detail. Here, we report the identification a
Publikováno v:
Applied Microbiology and Biotechnology, 83(4), 679-687. SPRINGER
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology
Streptomyces coelicolor A3(2) alditol oxidase (AldO) is a soluble monomeric flavoprotein in which the flavin cofactor is covalently linked to the polypeptide chain. AldO displays high reactivity towards different polyols such as xylitol and sorbitol.
Publikováno v:
Biochemical and Biophysical Research Communications, 362(3), 727-733. Academic Press Inc.
van Bloois, D W, ten Hagen-Jongman, C M & Luirink, S 2007, ' Flexibility in targeting and insertion during bacterial membrane protein biogenesis. ', Biochemical and Biophysical Research Communications, vol. 362, no. 3, pp. 727-733 . https://doi.org/10.1016/j.bbrc.2007.08.053
van Bloois, D W, ten Hagen-Jongman, C M & Luirink, S 2007, ' Flexibility in targeting and insertion during bacterial membrane protein biogenesis. ', Biochemical and Biophysical Research Communications, vol. 362, no. 3, pp. 727-733 . https://doi.org/10.1016/j.bbrc.2007.08.053
The biogenesis of Escherichia coli inner membrane proteins (IMPs) is assisted by targeting and insertion factors such as the signal recognition particle (SRP), the Sec-translocon and YidC with translocation of (large) periplasmic domains energized by
Autor:
Joen Luirink, Gregory Koningstein, Heike Bauerschmitt, Johannes M. Herrmann, Edwin van Bloois
Publikováno v:
FEBS Journal. 274:5704-5713
Members of the YidC/Oxa1/Alb3 protein family function in the biogenesis of membrane proteins in bacteria, mitochondria and chloroplasts. In Escherichia coli, YidC plays a key role in the integration and assembly of many inner membrane proteins. Inter
Publikováno v:
Journal of Biological Chemistry, 14(281). American Society for Biochemistry and Molecular Biology Inc.
van Bloois, D W, Haan, G J, de Gier, J-W, Oudega, B & Luirink, S 2006, ' Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. ', Journal of Biological Chemistry, vol. 14, no. 281 . https://doi.org/10.1074/jbc.M511357200
van Bloois, D W, Haan, G J, de Gier, J-W, Oudega, B & Luirink, S 2006, ' Distinct requirements for translocation of the N-tail and C-tail of the Escherichia coli inner membrane protein CyoA. ', Journal of Biological Chemistry, vol. 14, no. 281 . https://doi.org/10.1074/jbc.M511357200
Inner membrane proteins (IMPs) of Escherichia coli use different pathways for membrane targeting and integration. YidC plays an essential but poorly defined role in the integration and folding of IMPs both in conjunction with the Sec translocon and a
Publikováno v:
FEBS Letters. 576:97-100
Escherichia coli inner membrane proteins (IMPs) use different pathways for targeting and membrane integration. We have examined the biogenesis of the F1F0 ATP synthase subunit c, a small double spanning IMP, using complementary in vivo and in vitro a