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Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.
Philos Trans R Soc Lond B Biol Sci. 2012 Sep 19; 367(1602):2656-68.PT

Abstract

The switch between the Krebs cycle and the glyoxylate bypass is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK). AceK, a bifunctional enzyme, phosphorylates and dephosphorylates isocitrate dehydrogenase (IDH) with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities. AceK was the first example of prokaryotic phosphorylation identified, and the recent characterization of the structures of AceK and its complex with its protein substrate, IDH, now offers a new understanding of both previous and future endeavours. AceK is structurally similar to the eukaryotic protein kinase superfamily, sharing many of the familiar catalytic and regulatory motifs, demonstrating a close evolutionary relationship. Although the active site is shared by both the kinase and phosphatase functions, the catalytic residues needed for phosphatase function are readily seen when compared with the DXDX(T/V) family of phosphatases, despite the fact that the phosphatase function of AceK is strictly ATP/ADP-dependent. Structural analysis has also allowed a detailed look at regulation and its stringent requirements for interacting with IDH.

Authors+Show Affiliations

College of Chemistry, Beijing Normal University, Beijing 100875, People's Republic of China.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

22889914

Citation

Zheng, Jimin, et al. "Structural and Mechanistic Insights Into the Bifunctional Enzyme Isocitrate Dehydrogenase Kinase/phosphatase AceK." Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, vol. 367, no. 1602, 2012, pp. 2656-68.
Zheng J, Yates SP, Jia Z. Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK. Philos Trans R Soc Lond B Biol Sci. 2012;367(1602):2656-68.
Zheng, J., Yates, S. P., & Jia, Z. (2012). Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences, 367(1602), 2656-68. https://doi.org/10.1098/rstb.2011.0426
Zheng J, Yates SP, Jia Z. Structural and Mechanistic Insights Into the Bifunctional Enzyme Isocitrate Dehydrogenase Kinase/phosphatase AceK. Philos Trans R Soc Lond B Biol Sci. 2012 Sep 19;367(1602):2656-68. PubMed PMID: 22889914.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK. AU - Zheng,Jimin, AU - Yates,Susan P, AU - Jia,Zongchao, PY - 2012/8/15/entrez PY - 2012/8/15/pubmed PY - 2012/12/18/medline SP - 2656 EP - 68 JF - Philosophical transactions of the Royal Society of London. Series B, Biological sciences JO - Philos Trans R Soc Lond B Biol Sci VL - 367 IS - 1602 N2 - The switch between the Krebs cycle and the glyoxylate bypass is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK). AceK, a bifunctional enzyme, phosphorylates and dephosphorylates isocitrate dehydrogenase (IDH) with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities. AceK was the first example of prokaryotic phosphorylation identified, and the recent characterization of the structures of AceK and its complex with its protein substrate, IDH, now offers a new understanding of both previous and future endeavours. AceK is structurally similar to the eukaryotic protein kinase superfamily, sharing many of the familiar catalytic and regulatory motifs, demonstrating a close evolutionary relationship. Although the active site is shared by both the kinase and phosphatase functions, the catalytic residues needed for phosphatase function are readily seen when compared with the DXDX(T/V) family of phosphatases, despite the fact that the phosphatase function of AceK is strictly ATP/ADP-dependent. Structural analysis has also allowed a detailed look at regulation and its stringent requirements for interacting with IDH. SN - 1471-2970 UR - https://www.unboundmedicine.com/medline/citation/22889914/Structural_and_mechanistic_insights_into_the_bifunctional_enzyme_isocitrate_dehydrogenase_kinase/phosphatase_AceK_ L2 - https://royalsocietypublishing.org/doi/10.1098/rstb.2011.0426?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -