X-RAY CRYSTALLOGRAPHIC STUDIES OF METAL-REQUIRING ENZYMES

需要金属的酶的 X 射线晶体学研究

• 批准号: 8169239
• 负责人: DAVID W CHRISTIANSON
• 金额: $ 1.74万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169239
• 关键词: Amidohydrolases; Anabolism; Biology; Chemicals; Commit; Complex; Computer Retrieval of Information on Scientific Projects Database; Cyclization; Deacetylase; Enzymes; Evolution; Funding; Gram-Negative Bacteria; Grant; Histone Deacetylase; Human; Institution; Ions; Lipid A; Manganese; Metals; Organic Chemicals; Reaction; Research; Research Personnel; Resources; Site; Source; Specificity; Synchrotrons; System; Terpenes; United States National Institutes of Health; Work; Yersinia enterocolitica; Zinc; arginase; base; chemical reaction; delta-cadinene synthase; farnesyl pyrophosphate; metalloenzyme; mutant; stoichiometry; trichodiene synthase

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Our work at NE-CAT has focused on a number of metalloenzyme systems for which crystal quality and size make their study difficult at other synchrotron sources. A key project in the lab focuses on the binuclear manganese metalloezyme arginase, as well as enzymes that share the arginase fold such as the zinc enzymes human histone deacetylase-8 and bacterial acetylpolyamine amidohydrolase. This work additionally includes the zinc-dependent deacetylase LpxC from Yersinia enterocolitica, which catalyzes the first committed step of lipid A biosynthesis in Gram-negative bacteria. Comparisons of these metalloenzymes will ultimately reveal the chemical and structural basis for the divergent evolution of metal ion specificity and stoichiometry in the arginase fold. Additionally, our work at NE-CAT has focused on terpenoid cyclases. These are metal-requiring enzymes that catalyze the most complex organic chemical reactions in biology. Specifically, our work has focused on sesquiterpene cyclases that catalyze cyclization reactions involving the substrate farnesyl diphosphate: delta cadinene synthase and site-specific mutants of epi-isozizaene synthase.

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