Zobrazeno 1 - 10 of 19 pro vyhledávání: '"Wendy A. Doyle"'
1
Engineering Towards Catalytic Use of Fungal Class-II Peroxidases for Dye-Decolorizing and Conversion of Lignin Model Compounds
Autor: Andrew T. Smith, Kristiina Hildén, Johanna Rytioja, Matti Wahlsten, Jaana Kuuskeri, Taina Lundell, Usenobong F. Ufot, Paula Nousiainen, Wendy A. Doyle, Elodie Bentley, Martin Hofrichter
Publikováno v: Current Biotechnology. 6:116-127
Background. Manganese peroxidases (MnP) and lignin peroxidases (LiP) are haem-including fungal secreted class-II peroxidases, which are interesting oxidoreductases in protein engineering aimed at design of biocatalysts for lignin and lignocellulose c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae9eae79b929dd42750bce73cb1b792e
https://doi.org/10.2174/2211550105666160520120101
Zobrazit plný text záznamu
2
Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase
Autor: Pierre Dorlet, Wendy A. Doyle, Anabella Ivancich, Andrew T. Smith
Publikováno v: Proceedings of the National Academy of Sciences. 106:16084-16089
The surface oxidation site (Trp-171) in lignin peroxidase (LiP) required for the reaction with veratryl alcohol a high-redox-potential (1.4 V) substrate, was engineered into Coprinus cinereus peroxidase (CiP) by introducing a Trp residue into a heme
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0279f3a4cb77f7edef71730759bf66ef
https://doi.org/10.1073/pnas.0904535106
Zobrazit plný text záznamu
3
Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S. Evidence for selective effects on the reduced state of the enzyme
Autor: Wendy A. Doyle, Andrew T. Smith, Giulietta Smulevich, Barry D. Howes, Nigel C. Brissett
Publikováno v: FEBS Journal. 272:5514-5521
Studies on horseradish peroxidase C and other haem peroxidases have been carried out on selected mutants in the distal haem cavity providing insight into the functional importance of the distal residues. Recent work has demonstrated that proximal str
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba3a959e412e58c33f76b80336ccf72e
https://doi.org/10.1111/j.1742-4658.2005.04943.x
Zobrazit plný text záznamu
4
Expression of Pleurotus eryngii versatile peroxidase in Escherichia coli and optimisation of in vitro folding
Autor: María Jesús Martínez, Ángel T. Martínez, Francisco J. Ruiz-Dueñas, Marta Pérez-Boada, Andrew T. Smith, Wendy A. Doyle
Publikováno v: Enzyme and Microbial Technology. 30:518-524
Heterologous expression of Pleurotus eryngii versatile peroxidase (VP) in Escherichia coli was investigated. The cDNA encoding the mature sequence of the allelic variant VPL2 was cloned into the expression vector pFLAG1 and expressed in E. coli W3110
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b3c5baa141875c14184f2d22a91fd285
https://doi.org/10.1016/s0141-0229(02)00008-x
Zobrazit plný text záznamu
5
Two Substrate Interaction Sites in Lignin Peroxidase Revealed by Site-Directed Mutagenesis
Autor: Wendy A. Doyle, Klaus Piontek, Wolfgang Blodig, Nigel C. Veitch, Andrew T. Smith
Publikováno v: Biochemistry. 37:15097-15105
It has been shown recently that Trp171 of lignin peroxidase (LiP) is hydroxylated at the Cbeta position [Blodig, W., Doyle, W. A., Smith, A. T., Winterhalter, K., Choinowski, T., and Piontek, K. (1998) Biochemistry 37, 8832-8838]. Comparative experim
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6fad95692888aaa16619e329058d14b
https://doi.org/10.1021/bi981633h
Zobrazit plný text záznamu
6
Autocatalytic Formation of a Hydroxy Group at Cβ of Trp171 in Lignin Peroxidase
Autor: Klaus Piontek, Andrew T. Smith, Kaspar H. Winterhalter, Thomas Choinowski, Wendy A. Doyle, Wolfgang Blodig
Publikováno v: Biochemistry. 37:8832-8838
In the high-resolution crystal structures of two lignin peroxidase isozymes from the white rot fungus Phanerochaete chrysosporium a significant electron density at single bond distance from the C beta of Trp171 was observed and interpreted as a hydro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2029d1f15f2afa8b4d36e379d2438ea4
https://doi.org/10.1021/bi9727186
Zobrazit plný text záznamu
7
Properties of Xanthine Dehydrogenase Variants from Rosy Mutant Strains of Drosophila melanogaster and their Relevance to the enzyme's Structure and Mechanism
Autor: F. Lee Dutton, Robert C. Bray, Wendy A. Doyle, Julian F. Burke, J. Robert S. Whittle, Arthur Chovnick
Publikováno v: European Journal of Biochemistry. 239:782-795
Xanthine dehydrogenase, a molybdenum, iron-sulfur flavoenzyme encoded in the fruit fly Drosophila melanogaster by the rosy gene, has been characterised both from the wild-type and mutant files. Enzyme assays, using a variety of different oxidising an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d0ad9a5e9c583a8bc81382e4eba552b
https://doi.org/10.1111/j.1432-1033.1996.0782u.x
Zobrazit plný text záznamu
9
Properties of Rabbit Liver Aldehyde Oxidase and the Relationship of the Enzyme to Xanthine Oxidase and Dehydrogenase
Autor: Robert C. Bray, Wendy A. Doyle, Andrew M. Ventom, Nigel A. Turner
Publikováno v: European Journal of Biochemistry. 232:646-657
The properties of the molybdenum iron-sulfur flavoprotein, aldehyde oxidase from rabbit livers, have been further investigated in comparison with bovine milk xanthine oxidase. In agreement with earlier work, the ultraviolet/visible spectra indicate t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f813756aed68a2a5fd55a962a6bf283
https://doi.org/10.1111/j.1432-1033.1995.646zz.x
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje