Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site

Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site Descriptor: 4-hydroxy-2-oxovalerate aldolase, Acetaldehyde dehydrogenase, CHLORIDE ION, ... Authors: Fischer, B, Branlant, G, Talfournier, F, Gruez, A. Deposit date: 2013-07-20 Release date: 2013-09-04 Last modified: 2023-11-15 Method: X-RAY DIFFRACTION (1.55 Å) Cite: Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site To be Published

来自弯曲热单孢菌（Thermomonospora curvata）的双功能酶（醛缩酶/醛脱氢酶（Aldolase/Aldehyde dehydrogenase））的晶体与溶液结构，揭示了其在共享辅因子结合位点内容纳烟酰胺腺嘌呤二核苷酸（NAD+）与辅酶A（CoA）时的辅因子结合结构域运动。描述符：4-羟基-2-氧代戊酸醛缩酶、乙醛脱氢酶、氯离子（CHLORIDE ION）等。作者：Fischer, B、Branlant, G、Talfournier, F、Gruez, A。提交日期：2013年7月20日；发布日期：2013年9月4日；最后修改日期：2023年11月15日。实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率1.55埃（Å）。引用文献：来自弯曲热单孢菌（Thermomonospora curvata）的双功能酶（醛缩酶/醛脱氢酶）的晶体与溶液结构，揭示了在共享辅因子结合位点内结合NAD+与CoA过程中的辅因子结合结构域运动（待发表）