ACAT1 tetramer acetylates IDH2 dimer

Stable Identifier
R-HSA-9854415
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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All enzymes of the TCA cycle are highly acetylated at multiple lysine residues (reviewed in Zhao et al., 2010). The effects of this modification on enzyme activity are largely unknown. In the case of IDH2, however, acetylation by ACAT1 homotetramer at lysine 413 abolishes its activity (Chen et al., 2021), and thereby plays a major role in TCA cycle regulation.
Literature References
PubMed ID Title Journal Year
20167786 Regulation of cellular metabolism by protein lysine acetylation

An, W, Jiang, W, Hancock, SM, Zhou, L, Qin, L, Shi, J, Zeng, Y, Yao, J, Lin, Y, Zhao, S, Lei, Q, Xiong, Y, Chen, X, Guan, KL, Yu, W, Yang, P, Xu, W, He, F, Li, Y, Li, H, Zhang, T, Chin, J

Science 2010
34289383 Lysine acetylation restricts mutant IDH2 activity to optimize transformation in AML cells

Lonial, S, Su, R, Zhang, R, Mao, H, Wu, R, Fan, H, Wang, M, He, C, Xia, S, Elf, SE, Famulare, CA, Gao, X, Chen, J, Stock, W, Chen, J, Le Beau, M, Odenike, O, Chen, D, Blum, WG, Arellano, M, Zhu, AC, Levine, RL, Boggon, TJ, Li, Y, Dong, L

Mol Cell 2021
Participants
Participates
Catalyst Activity

acetyltransferase activity of ACAT1 tetramer [mitochondrial matrix]

Orthologous Events
Cross References
RHEA
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Reviewed
Created
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