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Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase.
FEBS Lett. 2016 09; 590(18):3144-54.FL

Abstract

This work aims to investigate the role of the loopβ3αC amino acids in the structure and function of isocitrate dehydrogenase kinase/phosphatase (AceK). The results demonstrate that the precise configuration of loopβ3αC is very important for AceK structure and function: structural changes alter the affinity of the enzyme for the isocitrate dehydrogenase (ICDH), which modifies enzyme activity. Intriguingly, D340 is significant for the retention of kinase and phosphatase activities, for the conformational stability of AceK and for binding ICDH. The deletion Δ341-345 increases enzyme activity by increasing the maximum velocity and affinity for ICDH. The β3αC loop is thus critical for the structure and function of AceK.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China.Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China.Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China.Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China.College of Chemistry, Beijing Normal University, China.College of Chemistry, Beijing Normal University, China.Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China. jgh982@bnu.edu.cn.Department of Biochemistry and Molecular Biology, Beijing Normal University, Beijing Key Laboratory, China. weiq@bnu.edu.cn.

Pub Type(s)

Letter
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

27528271

Citation

Yin, Yanxia, et al. "Loopβ3αC Plays an Important Role in the Structure and Function of Isocitrate Dehydrogenase Kinase/phosphatase." FEBS Letters, vol. 590, no. 18, 2016, pp. 3144-54.
Yin Y, Li S, Gao Y, et al. Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase. FEBS Lett. 2016;590(18):3144-54.
Yin, Y., Li, S., Gao, Y., Tong, L., Zheng, J., Jia, Z., Jiang, G., & Wei, Q. (2016). Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase. FEBS Letters, 590(18), 3144-54. https://doi.org/10.1002/1873-3468.12355
Yin Y, et al. Loopβ3αC Plays an Important Role in the Structure and Function of Isocitrate Dehydrogenase Kinase/phosphatase. FEBS Lett. 2016;590(18):3144-54. PubMed PMID: 27528271.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase. AU - Yin,Yanxia, AU - Li,Shanze, AU - Gao,Yadan, AU - Tong,Li, AU - Zheng,Jimin, AU - Jia,Zongchao, AU - Jiang,Guohua, AU - Wei,Qun, Y1 - 2016/08/28/ PY - 2016/03/01/received PY - 2016/08/02/revised PY - 2016/08/08/accepted PY - 2016/8/17/entrez PY - 2016/8/17/pubmed PY - 2017/5/13/medline KW - AceK KW - deletion mutant KW - isocitrate dehydrogenase KW - kinase KW - loop β3αC KW - phosphatase SP - 3144 EP - 54 JF - FEBS letters JO - FEBS Lett VL - 590 IS - 18 N2 - This work aims to investigate the role of the loopβ3αC amino acids in the structure and function of isocitrate dehydrogenase kinase/phosphatase (AceK). The results demonstrate that the precise configuration of loopβ3αC is very important for AceK structure and function: structural changes alter the affinity of the enzyme for the isocitrate dehydrogenase (ICDH), which modifies enzyme activity. Intriguingly, D340 is significant for the retention of kinase and phosphatase activities, for the conformational stability of AceK and for binding ICDH. The deletion Δ341-345 increases enzyme activity by increasing the maximum velocity and affinity for ICDH. The β3αC loop is thus critical for the structure and function of AceK. SN - 1873-3468 UR - https://www.unboundmedicine.com/medline/citation/27528271/Loopβ3αC_plays_an_important_role_in_the_structure_and_function_of_isocitrate_dehydrogenase_kinase/phosphatase_ L2 - https://doi.org/10.1002/1873-3468.12355 DB - PRIME DP - Unbound Medicine ER -