Summary
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1.
None of the six lysine residues of lysozyme forms part of its active center.
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2.
The lysine 6-NH2 groups of lysozyme are nonequivalent: three lie on the surface of the macromolecule, and the other three are hidden within the macromolecule. Blocking of the latter is always associated with breakdown of the structure of the protein and leads to the irreversible denaturing of the enzyme. These groups are probably necessary for the formation of internal bonds which maintain the native structure of the lysozyme molecule.
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3.
The irreversible deactivation of lysozyme by urea in an alkaline medium may arise from the action of urea as a chemical reagent in blocking the lysine 6-NH2 groups, which play the part of structure-forming elements.
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Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No. 5, pp. 830–838, May, 1965 Original article submitted September 8, 1964
This article is published in accordance with a resolution of the Conference of Chief Editors of Journals of the Academy of Sciences of the USSR of June 12, 1962, as a dissertation paper by G. V. Kleopina.
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Kleopina, G.V., Kravchenko, N.A. & Kaverzneva, E.D. Role of the 6-amino groups of lysine in lysozyme. Russ Chem Bull 14, 806–812 (1965). https://doi.org/10.1007/BF00845692
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DOI: https://doi.org/10.1007/BF00845692