Výsledky vyhledávání - "Jeremy Lohman"

Structures of chloramphenicol acetyltransferase III and E. coli β-ketoacylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(dethia)CoA

Autor: Lee Stunkard, Jianheng Ling, Aaron Benjamin, Jeremy Lohman, Jaelen Nice

Acetyl-CoA is a reactive metabolite that non-productively hydrolyzes in a number of enzyme active sites on the crystallization time frame. In order to elucidate enzyme:acetyl-CoA interactions leading to catalysis, acetyl-CoA substrate analogs are nee

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0029f079385e726918beaef44ac1e026
https://doi.org/10.1101/2022.08.24.505111

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Activity of fatty acid biosynthesis initiating ketosynthase FabH with acetyl/malonyl-oxa/aza(dethia)CoAs

Autor: Trevor Boram, Aaron Benjamin, Amanda Silva de Sousa, Lee Stunkard, Taylor Stewart, Timothy Adams, Nicholas Craft, Kevin Velázquez-Marrero, Jianheng Ling, Jaelen Nice, Jeremy Lohman

Fatty acid biosynthetic enzymes exploit the reactivity of acyl- and malonyl-thioesters for catalysis. Here we synthesize acetyl/malonyl-CoA analogs with esters or amides in place of the thioester and characterize their behavior as substrates or inhib

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::85e84d4f3a55c88a0408c5b45e8cd1d1
https://doi.org/10.26434/chemrxiv-2022-ww1zq

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Acetyl‐CoA Electron Density: Acyl‐CoA Reactivity and Crystallographic Data

Autor: Colin Hemme, Jeremy Lohman

Publikováno v: The FASEB Journal. 36

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::991466404b6f6d2bac2c5218ca22cabd
https://doi.org/10.1096/fasebj.2022.36.s1.r6285

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Abstract 1630: Cryo-EM structure of the E. coli acetyl-CoA carboxylase complex, forming an unprecedented tube-like filament

Autor: Jeremy Lohman, Amanda Sousa de Silva, Xueyong Xu, Wen Jiang

Publikováno v: Journal of Biological Chemistry. 299:103605

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::95f96b121b36f78625adbbd0f371702d
https://doi.org/10.1016/j.jbc.2023.103605

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Crystal Structures of Streptomyces Coelicolor Methylmalonyl-CoA Epimerase with Substrate or Transition State Analog Contradicts a Simple General Acid-Base Catalytic Mechanism

Autor: Jeremy Lohman, Tyler Huth, James Bower, Aaron B Benjamin, Lee M Stunkard

Crystal structures of Streptomyces coelicolor methylmalonyl-CoA epimerase in the holo-form, with substrate or the putative transition state analog, 2-nitroproionyl-CoA. The proposed catalytic mechanism is general acid-base catalysis. The proposed cat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8df9998b78867ba87b27f7ea1d36faae
https://doi.org/10.26434/chemrxiv.14403929

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