Crystallographic Capture of Quinolinate Synthase (NadA) from Pyrococcus horikoshii in its Substrates and Product-Bound States

Protein Data Bank Japan2026-08-12 更新2026-03-21 收录

喹啉酸合酶反应机制

酶-底物复合物结构

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Crystallographic Capture of Quinolinate Synthase (NadA) from Pyrococcus horikoshii in its Substrates and Product-Bound States Descriptor: DIDEHYDROASPARTATE, IRON/SULFUR CLUSTER, Quinolinate synthase A Authors: Esakova, O.A, Grove, T.L, Silakov, A, Yennawar, N.H, Booker, S.J. Deposit date: 2019-01-25 Release date: 2019-08-21 Last modified: 2026-08-12 Method: X-RAY DIFFRACTION (2.15 Å) Cite: An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase. J.Am.Chem.Soc., 141, 2019

数据集标题：来自激烈热球菌（Pyrococcus horikoshii）的喹啉酸合酶（Quinolinate Synthase，NadA）底物与产物结合状态的晶体捕获描述项：二氢天冬氨酸（DIDEHYDROASPARTATE）、铁硫簇（IRON/SULFUR CLUSTER）、喹啉酸合酶A（Quinolinate synthase A）作者：Esakova, O.A、Grove, T.L、Silakov, A、Yennawar, N.H、Booker, S.J. 存档日期：2019-01-25 发布日期：2019-08-21 最后修改日期：2024-03-13 实验方法：X射线衍射（X-RAY DIFFRACTION），分辨率2.15埃（Å）引用文献：《X射线晶体学确定的一种可能代表喹啉酸合酶催化反应中间体的新型物种》，《美国化学会志》，141卷，2019年

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2019-01-25

Crystallographic Capture of Quinolinate Synthase (NadA) from Pyrococcus horikoshii in its Substrates and Product-Bound States

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