The influence of the amino-acid substitution Arg486Cys on the conformational stability of recombinant cytochrome P450 7B1 (CYP7B1, oxysterol 7α-hydroxylase) was studied. The single base change was shown to decrease the free energy of the transition of the heme-protein from its native state to a denatured one, which pointed to a lower thermodynamic stability for the mutant form of the enzyme. This could be the cause of the metabolic disruption of neurosteroids and, as a consequence, the appearance of neurodegenerative diseases.
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 82, No. 1, pp. 96–102, January–February, 2015.
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Dichenko, Y.V., Yantsevich, A.V. & Usanov, S.A. Structural and Functional Characteristics of Oxysterol 7α-Hydroxylase with Amino-Acid Substitution R486C and Their Relation to the Appearance of Neurodegenerative Diseases. J Appl Spectrosc 82, 91–97 (2015). https://doi.org/10.1007/s10812-015-0069-0
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DOI: https://doi.org/10.1007/s10812-015-0069-0