Výsledky vyhledávání - "Lauris E. Kemp"

Crystallization and preliminary X-ray diffraction studies of recombinantEscherichia coli4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase

Autor: William N. Hunter, Charles S. Bond, Lauris E. Kemp

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 57:1189-1191

Diphosphocytidyl-methylerythritol (DPCME) synthetase is involved in the mevalonate-independent pathway of isoprenoid biosynthesis, where it catalyses the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6204ec6690e221e3a8b3e2504177fcdb
https://doi.org/10.1107/s0907444901010137

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A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate

Autor: Tanja Sgraja, Nicola L. Ramsden, William N. Hunter, Lauris E. Kemp

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 7)

The essential enzyme 2C-methyl-d-erythritol-2,4-cyclodiphosphate (MECP) synthase, found in most eubacteria and the apicomplexan parasites, participates in isoprenoid-precursor biosynthesis and is a validated target for the development of broad-spectr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4fc08a522dc7490ad43a6618451aef0
https://pubmed.ncbi.nlm.nih.gov/16511114

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The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods

Autor: Michael A. J. Ferguson, Wolfgang Eisenreich, Felix Rohdich, William N. Hunter, Stefan Hecht, Charles S. Bond, Adelbert Bacher, Magnus S. Alphey, Lauris E. Kemp

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 61(Pt 1)

The discovery of a distinct metabolic pathway, the non-mevalonate or 1-deoxy-d-xylulose-5-phosphate (DOXP) pathway for isoprenoid precursor biosynthesis, in eubacteria and apicomplexan parasites has revealed a new set of potential drug targets. The e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20369ed7042fb404ea8807c7c97fde82
https://pubmed.ncbi.nlm.nih.gov/15608374

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Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase

Autor: Felix Rohdich, William N. Hunter, Wolfgang Eisenreich, Stefan Hecht, Sean McSweeney, Linda Miallau, Gordon A. Leonard, Adelbert Bacher, Magnus S. Alphey, Lauris E. Kemp

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 100(16)

4-Diphosphocytidyl-2 C -methyl- d -erythritol kinase, an essential enzyme in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, catalyzes the single ATP-dependent phosphorylation stage affording 4-diphosp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1484d3ee898055be5d03c90a7c17fc21
https://pubmed.ncbi.nlm.nih.gov/12878729

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Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Autor: Charles S. Bond, William N. Hunter, Lauris E. Kemp

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 59(Pt 3)

2-C-Methyl-d-erythritol 4-phosphate cytidylyltransferase is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. The structure of a tetragonal crystal form has been solved by molecular replacement and refined to 2.4 A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d14111fc57e5fc85f915550ed56d231
https://pubmed.ncbi.nlm.nih.gov/12595740

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Crystal structure of an enzyme involved in the biosynthesis of isoprenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol kinase fromE. coli, a potential drug target

Autor: Wolfgang Eisenreich, Linda Miallau, Lauris E. Kemp, and Adelbert Bacher, Sean McSweeney, Gordon A. Leonard, William N. Hunter, Stefan Hecht, Felix Rohdich, Magnus S. Alphey

Publikováno v: Acta Crystallographica Section A Foundations of Crystallography. 61:c188-c188

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9cf248a4d1496fbaeb7c0466075c4a99
https://doi.org/10.1107/s0108767305092007

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Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis

Autor: Charles S. Bond, William N. Hunter, Mads Gabrielsen, Lauris E. Kemp

Publikováno v: ResearcherID

The function, structure and mechanism of two Escherichia coli enzymes involved in the non-mevalonate route of isoprenoid biosynthesis, 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase and 2C-methyl-d-erythritol 2,4-cyclodiphosphate synthase, a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f481696c27646b0508de52295dd2867
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000183622500012&KeyUID=WOS:000183622500012

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