Abstract
In order to understand enzyme catalysis it is necessary to know the specific spatial arrangement of the active site amino acid side chains. By interaction with each other or with a coenzyme the functional groups of the active site form a sort of polar complex which enables the formation of the transition state of the enzyme substrate complex. However, because of the flexibility of the protein structure, equilibria of these manifold interactions have to be considered. If a distinct interaction between two side chains is needed for the catalytic activity, only the enzyme species with this interaction is active, whereas all other species should be inactive.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Dwek RA (1973) Nuclear magnetic resonance in biochemistry, application to enzyme systems. Claredon Press, Oxford
Blomberg F, Maurer W, Rüterjans H (1977) J Am Chem Soc 99: 8149
Bachovchin WW, Roberts JD (1978) J Am Chem Soc 100: 8041
Blow DM, Steitz TA, (1970): Ann Rev. Biochem 39: 63
Rüterjans H, Witzel H (1969) Eur J Biochem 9: 118
Haar W, Thompson JC, Maurer W, Rüterjans H (1973) Eur J Biochem 40: 259
Haar W, Maurer W, Rüterjans H (1974) Eur J Biochem 44: 201
Richards FM, Wyckoff HW (1971) In: Boyer BD (ed) The enzymes, vol IV. Academic Press, London New York, p 647
Büchner P, Blomberg F, Rüterjans H (1978) In: Pallman B (ed) Nuclear magnetic resonance spectroscopy in molecular biology. D Reidel Publ Comp, Dordrecht, Holland, p 53
Wyman J (1964) Adv Protein Chem 19: 224
Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 89
Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 79
Steigemann W, Weber E (1979) J Mol Biol 127: 309; Huber R, Epp O, Steigemann W, Formanek H (1971) Eur J Biochem 19: 32
Krümpelmann D, Ribbing W, Rüterjans H (1980) Eur J Biochem 108: 103
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1981 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Rüterjans, H. (1981). NMR in the Study of Enzyme Catalysis. In: Eggerer, H., Huber, R. (eds) Structural and Functional Aspects of Enzyme Catalysis. Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81738-0_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-81738-0_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-81740-3
Online ISBN: 978-3-642-81738-0
eBook Packages: Springer Book Archive