Allosteric Control of N-Acetyl-Aspartate Hydrolysis by the Y231C and F295S Mutants of Human Aspartoacylase-Reference-Cited by-同舟云学术

Allosteric Control of N-Acetyl-Aspartate Hydrolysis by the Y231C and F295S Mutants of Human Aspartoacylase

Published:2018-11-15 Issue:5 Volume:59 Page:2299-2308
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Kots Ekaterina D.¹²,Khrenova Maria G.¹³^ORCID,Nemukhin Alexander V.¹²^ORCID

Affiliation:

1. Department of Chemistry, Lomonosov Moscow State University, Leninskie Gory 1/3, Moscow, 119991, Russian Federation

2. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Kosygina 4, Moscow, 119334, Russian Federation

3. Federal Research Center of Biotechnology, Bach Institute of Biochemistry, Russian Academy of Sciences, Leninskiy Prospect 33, 119071 Moscow, Russian Federation

Funder

Russian Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.8b00666

Reference38 articles.

1. Proton MR spectroscopy in multiple sclerosis: value in establishing diagnosis, monitoring progression, and evaluating therapy.

2. Defective N-acetylaspartate catabolism reduces brain acetate levels and myelin lipid synthesis in Canavan's disease

3. Molecular basis of Canavan disease

4. Novel missense mutation (Y231C) in a Turkish patient with Canavan disease

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