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Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.
Biochemistry. 2011 Sep 27; 50(38):8103-6.B

Abstract

Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria.

Authors+Show Affiliations

Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21870819

Citation

Yates, Susan P., et al. "Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/phosphatase." Biochemistry, vol. 50, no. 38, 2011, pp. 8103-6.
Yates SP, Edwards TE, Bryan CM, et al. Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase. Biochemistry. 2011;50(38):8103-6.
Yates, S. P., Edwards, T. E., Bryan, C. M., Stein, A. J., Van Voorhis, W. C., Myler, P. J., Stewart, L. J., Zheng, J., & Jia, Z. (2011). Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase. Biochemistry, 50(38), 8103-6. https://doi.org/10.1021/bi200809p
Yates SP, et al. Structural Basis of the Substrate Specificity of Bifunctional Isocitrate Dehydrogenase Kinase/phosphatase. Biochemistry. 2011 Sep 27;50(38):8103-6. PubMed PMID: 21870819.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase. AU - Yates,Susan P, AU - Edwards,Thomas E, AU - Bryan,Cassie M, AU - Stein,Adam J, AU - Van Voorhis,Wesley C, AU - Myler,Peter J, AU - Stewart,Lance J, AU - Zheng,Jimin, AU - Jia,Zongchao, Y1 - 2011/09/02/ PY - 2011/8/30/entrez PY - 2011/8/30/pubmed PY - 2011/11/9/medline SP - 8103 EP - 6 JF - Biochemistry JO - Biochemistry VL - 50 IS - 38 N2 - Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria. SN - 1520-4995 UR - https://www.unboundmedicine.com/medline/citation/21870819/Structural_basis_of_the_substrate_specificity_of_bifunctional_isocitrate_dehydrogenase_kinase/phosphatase_ L2 - https://doi.org/10.1021/bi200809p DB - PRIME DP - Unbound Medicine ER -