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Russian Chemical Reviews, 2019, Volume 88, Issue 1, Pages 1–26
DOI: https://doi.org/10.1070/RCR4842
(Mi rcr4238)
 

This article is cited in 7 scientific papers (total in 7 papers)

Aspartoacylase: a central nervous system enzyme. Structure, catalytic activity and regulation mechanisms

E. D. Kotsab, M. G. Khrenovaac, A. V. Nemukhinab, S. D. Varfolomeevab

a Lomonosov Moscow State University, Faculty of Chemistry
b Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow
c Federal Research Centre "Fundamentals of Biotechnology" Russian Academy of Sciences, Moscow
English full-text Citations (7)
Abstract: Aspartoacylase is a key enzyme in the human central nervous system. Catalytic deficiency of aspartoacylase is associated with several neurodegenerative disorders, which accounts for the enhanced interest in description of the catalytic action and regulatory mechanisms of this enzyme. This review focuses on molecular modelling of the catalytic function of aspartoacylase and the ways of its allosteric regulation in terms of modern theoretical chemistry approaches. The conclusions based on experimental data on the structure and functions of aspartoacylase accumulated during the last 20 years and conclusions drawn from computer modelling results of the last 5 years are analyzed in detail.
The bibliography includes 109 references.
Funding agency Grant number
Russian Science Foundation 18-13-00030
Received: 08.06.2018
Russian version:
Uspekhi Khimii, 2019, Volume 88, Issue 1, Pages 1–26
DOI: https://doi.org/10.1070/RCR4842
Bibliographic databases:
Document Type: Article
Language: English
Original paper language: Russian
Citation: E. D. Kots, M. G. Khrenova, A. V. Nemukhin, S. D. Varfolomeev, “Aspartoacylase: a central nervous system enzyme. Structure, catalytic activity and regulation mechanisms”, Usp. Khim., 88:1 (2019), 1–26; Russian Chem. Reviews, 88:1 (2019), 1–26
Citation in format AMSBIB
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\jour Usp. Khim.
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\pages 1--26
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  • https://doi.org/10.1070/RCR4842
  • https://www.mathnet.ru/eng/rcr/v88/i1/p1
  • This publication is cited in the following 7 articles:
    Citing articles in Google Scholar: Russian citations, English citations
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