Výsledky vyhledávání - "Matthew Bycroft"

Development of a Chemoenzymatic Process for Dehydroepiandrosterone Acetate Synthesis

Autor: Nichola L. Davies, Srinivas Reddy Poreddy, Srikanth Sarat Chandra Gorantla, Vilas Hareshwar Dahanukar, D. Naresh Kumar Reddy, Karen E. Holt-Tiffin, George Evans, Justine Ann Peterson, Colin Dewar, Matthew Bycroft, Neil Triggs, Upadhya Timmanna, Michael Siegfried Quirmbach, Anna Fryszkowska, Toni Fleming, Garrett Hoge

Publikováno v: Organic Process Research & Development. 20:1520-1528

Dehydroepiandrosterone (DHEA, 2) is an important endogenous steroid hormone in mammals used in the treatment of a variety of dysfunctions in female and male health,1 as well as an intermediate in the synthesis of steroidal drugs, such as abiraterone

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5d4657f88c412058c784253d300e8e18
https://doi.org/10.1021/acs.oprd.6b00215

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Efficient purification and kinetic characterization of a bimodular derivative of the erythromycin polyketide synthase

Autor: Kira J. Weissman, Peter F. Leadlay, Matthew Bycroft, James Staunton

Publikováno v: European Journal of Biochemistry. 267:520-526

Modular polyketide synthases (PKSs), such as the 6-deoxyerythronolide B synthase (DEBS), are giant multienzymes that biosynthesize a number of clinically important natural products. The modular nature of PKSs suggests the possibility of a combinatori

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0c4733653ecc88aa26cceabbbd04b5a0
https://doi.org/10.1046/j.1432-1327.2000.01025.x

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Origin of Starter Units for Erythromycin Biosynthesis

Autor: James Staunton, Kira J. Weissman, Peter F. Leadlay, Matthew Bycroft

Publikováno v: Biochemistry. 37:11012-11017

Modular polyketide synthases (PKSs), such as the 6-deoxyerythronolide B synthase (DEBS), are multifunctional proteins that govern the synthesis of a number of clinically important natural products. The modular arrangement of active sites within these

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc6a91f7865a8dc0ec7617a375eca3e5
https://doi.org/10.1021/bi9806246

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The Thioesterase of the Erythromycin-Producing Polyketide Synthase: Influence of Acyl Chain Structure on the Mode of Release of Substrate Analogues from the Acyl Enzyme Intermediates

Autor: Kira J. Weissman, Peter F. Leadlay, Matthew Bycroft, Ranjana Aggarwal, James Staunton, Cameron J. Smith, Ulf Hanefeld

Publikováno v: Angewandte Chemie International Edition. 37:1437-1440

The production of genetically engineered polyketides depends critically on thioesterase activity for product release. In vitro studies with the thioesterase from the erythromycin polyketide synthase (PKS) have demonstrated that the ability of this en

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::adc6f21ffea07a993ea8dc390a029ecd
https://doi.org/10.1002/(sici)1521-3773(19980605)37:10<1437::aid-anie1437>3.0.co

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Die Thioesterase der Polyketid-Synthase von Erythromycin: Einfluß der Acylkettenstruktur auf den Abkopplungsmechanismus der Substratanaloga von der Acyl-Enzym-Zwischenstufe

Autor: Ulf Hanefeld, Ranjana Aggarwal, Kira J. Weissman, Peter F. Leadlay, James Staunton, Matthew Bycroft, Cameron J. Smith

Publikováno v: Angewandte Chemie. 110:1503-1506

Fur die gentechnische Herstellung von Polyketiden ist die Aktivitat der Thioesterase zur Abkopplung des Produkts von entscheidender Bedeutung. In-vitro-Studien mit der Thioesterase der Polyketid-Synthase (PKS) fur Erythromycin ergaben, das die Fahigk

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::42f03ff6db8a618532d38de4fcba70ca
https://doi.org/10.1002/(sici)1521-3757(19980518)110:10<1503::aid-ange1503>3.0.co

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The Molecular Basis of Celmer's Rules: The Stereochemistry of the Condensation Step in Chain Extension on the Erythromycin Polyketide Synthase

Autor: Ulf Hanefeld, James Staunton, Kira J. Weissman, Peter F. Leadlay, Matthew Bycroft, Peter Grice, Máire C. Timoney

Publikováno v: Biochemistry. 36:13849-13855

Modular polyketide synthases (PKSs), for example, the 6-deoxyerythronolide B synthase (DEBS) responsible for synthesis of the aglycone core of the macrolide antibiotic erythromycin, generate an impressive diversity of asymmetric centers in their poly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ffca678619a97133d4200347d18fc46
https://doi.org/10.1021/bi971566b

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Heterocyclic β-hydroxy-α-amino acids as substrates for a novel aldolase from Streptomyces amakusaensis; preparation of (2R,3R)-3-(2-thienyl)serine and (2R,3R)-3-(2-furyl)serine from racemic threo material

Autor: Richard B. Herbert, G. J. Ellames, Matthew Bycroft

Publikováno v: J. Chem. Soc., Perkin Trans. 1. :2439-2442

A novel aldolase from Streptomyces amakusaensis which catalyses a reverse aldol reaction on (2S,3R)-β-hydroxy-α-amino acids is specific for aromatic compounds, but otherwise shows broad substrate tolerance. This is further illustrated by its abilit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a54a76ba6785ce36001de1485c3af71a
https://doi.org/10.1039/p19960002439

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ChemInform Abstract: Heterocyclic β-Hydroxy-α-amino Acids as Substrates for a Novel Aldolase from Streptomyces amakusaensis: Preparation of (2R,3R)- 3-(2-Thienyl)serine and (2R,3R)-3-(2-Furyl)serine from Racemic threo Material

Autor: Matthew Bycroft, Richard B. Herbert, G. J. Ellames

Publikováno v: ChemInform. 28

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::880e5f42d365db66d932d2a43d61c85e
https://doi.org/10.1002/chin.199716048

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Knowledge-based design of bimodular and trimodular polyketide synthases based on domain and module swaps: a route to simple statin analogues

Autor: Anand Ranganathan, Matthew Bycroft, Ian S. Galloway, Iain P Thomas, Laurenz Kellenberger, Jesus Cortes, Barrie Wilkinson, Ulf Hanefeld, Peter F. Leadlay, Máire C. Timoney, James Staunton

Publikováno v: Chemistrybiology. 6(10)

Background: Polyketides are structurally diverse natural products that have a range of medically useful activities. Nonaromatic bacterial polyketides are synthesised on modular polyketide synthase (PKS) multienzymes, in which each cycle of chain exte

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94cdf45ae2e6da33403a9a7af390bc5f
https://pubmed.ncbi.nlm.nih.gov/10508677

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Molecular basis of Celmer's rules: the role of two ketoreductase domains in the control of chirality by the erythromycin modular polyketide synthase

Autor: Rebecca C. Harris, James Staunton, Jesus Cortes, Inès E. Holzbaur, Matthew Bycroft, Peter F. Leadlay, Brian A.M. Rudd, Christian Bisang

Publikováno v: Chemistrybiology. 6(4)

Background Polyketides are compounds that possess medically significant activities. The modular nature of the polyketide synthase (PKS) multienzymes has generated interest in bioengineering new PKSs. Rational design of novel PKSs, however, requires a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24a6ce1dbed7822ed2ce12fa54c07d36
https://pubmed.ncbi.nlm.nih.gov/10099131

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