SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM)
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SUPERSTABLE E65Q MUTANT OF LEISHMANIA MEXICANA TRIOSEPHOSPHATE ISOMERASE (TIM) Descriptor: 2-PHOSPHOGLYCOLIC ACID, TRIOSEPHOSPHATE ISOMERASE Authors: Lambeir, A.M, Backmann, J, Ruiz-Sanz, J, Filimonov, V, Nielsen, J.E, Vriend, G, Kursula, I, Norledge, B.V, Wierenga, R.K. Deposit date: 1999-07-10 Release date: 2000-12-13 Last modified: 2024-02-14 Method: X-RAY DIFFRACTION (2 Å) Cite: The ionization of a buried glutamic acid is thermodynamically linked to the stability of Leishmania mexicana triose phosphate isomerase. Eur.J.Biochem., 267, 2000
墨西哥利什曼原虫(Leishmania mexicana)磷酸丙糖异构酶(triosephosphate isomerase,TIM)的超稳定E65Q突变体
描述项:2-磷酸乙醇酸(2-PHOSPHOGLYCOLIC ACID)、磷酸丙糖异构酶
作者:Lambeir, A.M、Backmann, J、Ruiz-Sanz, J、Filimonov, V、Nielsen, J.E、Vriend, G、Kursula, I、Norledge, B.V、Wierenga, R.K
提交日期:1999-07-10
发布日期:2000-12-13
最后修改日期:2024-02-14
实验方法:X射线衍射(X-RAY DIFFRACTION),分辨率2 Å
引用文献:埋藏谷氨酸的电离作用与墨西哥利什曼原虫磷酸丙糖异构酶的稳定性存在热力学关联。《欧洲生物化学杂志》(Eur.J.Biochem.),267卷,2000年
创建时间:
1999-07-10



