Výsledky vyhledávání - "Heather A. Gennadios"

Crystal Structure of (+)-δ-Cadinene Synthase from Gossypium arboreum and Evolutionary Divergence of Metal Binding Motifs for Catalysis

Autor: David W. Christianson, Luigi Di Costanzo, Rudolf Konrad Allemann, Amang Li, Heather A. Gennadios, David James Miller, Veronica Gonzalez, Fanglei Yu

Publikováno v: Biochemistry. 48:6175-6183

(+)-Delta-cadinene synthase (DCS) from Gossypium arboreum (tree cotton) is a sesquiterpene cyclase that catalyzes the cyclization of farnesyl diphosphate in the first committed step of the biosynthesis of gossypol, a phytoalexin that defends the plan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9f509373acab66fab96164da2d17800
https://doi.org/10.1021/bi900483b

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Amphipathic benzoic acid derivatives: Synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC

Autor: Hyunshun Shin, David W. Christianson, Heather A. Gennadios, Douglas A. Whittington

Publikováno v: Bioorganic & Medicinal Chemistry. 15:2617-2623

The first committed step in lipid A biosynthesis is catalyzed by uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase (LpxC), a zinc-dependent deacetylase, and inhibitors of LpxC may be useful in the development of antibac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bf39fd85c8a58413497e28dbb6ce409
https://doi.org/10.1016/j.bmc.2007.01.044

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Mechanistic Inferences from the Binding of Ligands to LpxC, a Metal-Dependent Deacetylase

Autor: David W. Christianson, Heather A. Gennadios, Douglas A. Whittington, Xuechen Li, Carol A. Fierke

Publikováno v: Biochemistry. 45:7940-7948

The metal-dependent deacetylase LpxC catalyzes the first committed step of lipid A biosynthesis in Gram-negative bacteria. Accordingly, LpxC is an attractive target for the development of inhibitors that may serve as potential new antibiotics for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8adb84764b16afba2bebd0568c4c005
https://doi.org/10.1021/bi060823m

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UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine Deacetylase Functions through a General Acid-Base Catalyst Pair Mechanism

Autor: Carol A. Fierke, David W. Christianson, Marcy Hernick, Heather A. Gennadios, Douglas A. Whittington, Kristin M. Rusche

Publikováno v: Journal of Biological Chemistry. 280:16969-16978

UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1eb4d53b2789711e34bc244db406ceac
https://doi.org/10.1074/jbc.m413560200

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Binding of uridine 5'-diphosphate in the 'basic patch' of the zinc deacetylase LpxC and implications for substrate binding

Autor: David W. Christianson, Heather A. Gennadios

Publikováno v: Biochemistry. 45(51)

The zinc metalloenzyme UDP –{3-O-[(R)-3-hydroxymyristoyl]}-N-acetylglucosamine deacetylase (LpxC) catalyzes the first irreversible step in the biosynthesis of lipid A (Figure 1) (1-4), which is ultimately incorporated into the outer leaflet of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bede62f5e6df76cb90a897fb55aa1eb
https://pubmed.ncbi.nlm.nih.gov/17176043

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