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Two sides of the same coin: How enzymes distort substrates and vice versa. An infrared spectroscopic view on pyruvate kinase and Ca2+-ATPase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 1
2016 (English)In: Biomedical Spectroscopy and Imaging, ISSN 2212-8794, Vol. 5, no 2, 101-114 p.Article in journal (Refereed) Published
Abstract [en]

This review summarises our infrared spectroscopy and density functional theory studies on the mutual interactions between enzymes and their substrates. We investigated phosphoenolpyruvate bound to pyruvate kinase (EC, M1 isozyme), ATP bound to the Ca2+-ATPase (SERCA1a), and the aspartylphosphate moiety of the Ca2+-ATPase phosphoenzyme E2P. Conformational changes of the enzymes and distortions of substrate structure are discussed. In all cases, the infrared absorption of the substrate in the enzyme environment could be identified by a combination of reaction-induced difference spectroscopy and isotopic labelling. The experimentally-determined vibrational frequencies were interpreted in structural terms using experimental correlations or modelling of the active site in density functional theory calculations. For none of the three systems, a weakening of the bond that is cleaved in the following enzymatic reaction could be detected in the ground state of the enzyme-substrate complex. However, for the dephosphorylation reaction of the Ca2+-ATPase phosphoenzyme E2P, a high energy intermediate, not detected in experiments, is the reactant state according to density functional theory calculations.

Place, publisher, year, edition, pages
2016. Vol. 5, no 2, 101-114 p.
Keyword [en]
Conformational change, drug development, enzyme mechanism, FTIR spectroscopy, ground state destabilisation, infrared spectroscopy, phosphoenolpyruvate, phosphoenzyme, phosphate transfer, phosphorylation, pyruvate kinase, SERCA1a, substrate distortion, vibrational spectroscopy
National Category
Other Engineering and Technologies
URN: urn:nbn:se:su:diva-130015DOI: 10.3233/BSI-160134ISI: 000373502500002OAI: diva2:927054
Available from: 2016-05-10 Created: 2016-05-09 Last updated: 2016-07-06Bibliographically approved

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Barth, Andreas
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Department of Biochemistry and Biophysics
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