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Loopβ3αC plays an important role in the structure and function of isocitrate dehydrogenase kinase/phosphatase
Author(s) -
Yin Yanxia,
Li Shanze,
Gao Yadan,
Tong Li,
Zheng Jimin,
Jia Zongchao,
Jiang Guohua,
Wei Qun
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12355
Subject(s) - isocitrate dehydrogenase , phosphatase , enzyme , biochemistry , function (biology) , dehydrogenase , chemistry , protein phosphatase 2 , biology , microbiology and biotechnology
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.