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Journal Article

Structural relationships in the adenylate kinase family

MPS-Authors
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Brune,  Martin
Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95966

Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

External Resource

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1986.tb10132.x
(Any fulltext)

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1986.tb10132.x
(Any fulltext)

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Citation

Schulz, G. E., Schiltz, E., Tomasselli, A. G., Frank, R., Brune, M., Wittinghofer, A., et al. (1986). Structural relationships in the adenylate kinase family. European Journal of Biochemistry, 161(1), 127-132. doi:10.1111/j.1432-1033.1986.tb10132.x.


Cite as: https://hdl.handle.net/21.11116/0000-0006-9F32-F
Abstract
The sequences of five distantly related adenylate kinases have been aligned. The local conservation of amino acids is discussed in the light of the known three-dimensional structure of one of the enzymes, the cytosolic isoenzyme 1 (AK1) from porcine muscle. The similarity profile outlines clearly the active site in the cleft of the spatial structure of AK1. The alignment reveals further that the enzyme family can be subdivided into small and large variants according to the presence or absence of a particular segment of about 30 residues in the middle of the chain. The extra segments of the large variants are strongly conserved