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Unique kinase catalytic mechanism of AceK with a single magnesium ion.
PLoS One. 2013; 8(8):e72048.Plos

Abstract

Isocitrate dehydrogenase kinase/phosphatase (AceK) is the founding member of the protein phosphorylation system in prokaryotes. Based on the novel and unique structural characteristics of AceK recently uncovered, we sought to understand its kinase reaction mechanism, along with other features involved in the phosphotransfer process. Herein we report density functional theory QM calculations of the mechanism of the phosphotransfer reaction catalysed by AceK. The transition states located by the QM calculations indicate that the phosphorylation reaction, catalysed by AceK, follows a dissociative mechanism with Asp457 serving as the catalytic base to accept the proton delivered by the substrate. Our results also revealed that AceK prefers a single Mg(2+)-containing active site in the phosphotransfer reaction. The catalytic roles of conserved residues in the active site are discussed.

Authors+Show Affiliations

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

Pub Type(s)

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

Language

eng

PubMed ID

23977203

Citation

Li, Quanjie, et al. "Unique Kinase Catalytic Mechanism of AceK With a Single Magnesium Ion." PloS One, vol. 8, no. 8, 2013, pp. e72048.
Li Q, Zheng J, Tan H, et al. Unique kinase catalytic mechanism of AceK with a single magnesium ion. PLoS One. 2013;8(8):e72048.
Li, Q., Zheng, J., Tan, H., Li, X., Chen, G., & Jia, Z. (2013). Unique kinase catalytic mechanism of AceK with a single magnesium ion. PloS One, 8(8), e72048. https://doi.org/10.1371/journal.pone.0072048
Li Q, et al. Unique Kinase Catalytic Mechanism of AceK With a Single Magnesium Ion. PLoS One. 2013;8(8):e72048. PubMed PMID: 23977203.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Unique kinase catalytic mechanism of AceK with a single magnesium ion. AU - Li,Quanjie, AU - Zheng,Jimin, AU - Tan,Hongwei, AU - Li,Xichen, AU - Chen,Guangju, AU - Jia,Zongchao, Y1 - 2013/08/19/ PY - 2013/05/20/received PY - 2013/07/06/accepted PY - 2013/8/27/entrez PY - 2013/8/27/pubmed PY - 2014/4/9/medline SP - e72048 EP - e72048 JF - PloS one JO - PLoS One VL - 8 IS - 8 N2 - Isocitrate dehydrogenase kinase/phosphatase (AceK) is the founding member of the protein phosphorylation system in prokaryotes. Based on the novel and unique structural characteristics of AceK recently uncovered, we sought to understand its kinase reaction mechanism, along with other features involved in the phosphotransfer process. Herein we report density functional theory QM calculations of the mechanism of the phosphotransfer reaction catalysed by AceK. The transition states located by the QM calculations indicate that the phosphorylation reaction, catalysed by AceK, follows a dissociative mechanism with Asp457 serving as the catalytic base to accept the proton delivered by the substrate. Our results also revealed that AceK prefers a single Mg(2+)-containing active site in the phosphotransfer reaction. The catalytic roles of conserved residues in the active site are discussed. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/23977203/Unique_kinase_catalytic_mechanism_of_AceK_with_a_single_magnesium_ion_ L2 - https://dx.plos.org/10.1371/journal.pone.0072048 DB - PRIME DP - Unbound Medicine ER -