Roles of Intramolecular and Intermolecular Hydrogen Bonding in a Three-Water-Assisted Mechanism of Succinimide Formation from Aspartic Acid Residues

Autor: Ohgi Takahashi, Ryota Kirikoshi, Noriyoshi Manabe

Publikováno v: Molecules, Vol 19, Iss 8, Pp 11440-11452 (2014)

Aspartic acid (Asp) residues in peptides and proteins are prone to isomerization to the β-form and racemization via a five-membered succinimide intermediate. These nonenzymatic reactions have relevance to aging and age-related diseases. In this pape

Externí odkaz: https://doaj.org/article/58a896699a1c46ff883ee4f0ecc7506b

Racemization of the Succinimide Intermediate Formed in Proteins and Peptides: A Computational Study of the Mechanism Catalyzed by Dihydrogen Phosphate Ion

Autor: Ohgi Takahashi, Ryota Kirikoshi, Noriyoshi Manabe

Publikováno v: International Journal of Molecular Sciences, Vol 17, Iss 10, p 1698 (2016)

In proteins and peptides, d-aspartic acid (d-Asp) and d-β-Asp residues can be spontaneously formed via racemization of the succinimide intermediate formed from l-Asp and l-asparagine (l-Asn) residues. These biologically uncommon amino acid residues

Externí odkaz: https://doaj.org/article/df24e539f0454f539b346a11f2dea714

Phosphate-Catalyzed Succinimide Formation from Asp Residues: A Computational Study of the Mechanism

Autor: Ohgi Takahashi, Noriyoshi Manabe, Ryota Kirikoshi

Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences; Volume 19; Issue 2; Pages: 637
International Journal of Molecular Sciences, Vol 19, Iss 2, p 637 (2018)

Aspartic acid (Asp) residues in proteins and peptides are prone to the non-enzymatic reactions that give biologically uncommon l-β-Asp, d-Asp, and d-β-Asp residues via the cyclic succinimide intermediate (aminosuccinyl residue, Suc). These abnormal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81da5d7f812f9f82b3edfa656661c9a2
https://pubmed.ncbi.nlm.nih.gov/29495268

Conformational dependence of the intrinsic acidity of the aspartic acid residue sidechain in N-acetyl-l-aspartic acid-N′-methylamide

Autor: Janice S.W. Lam, Julius Gy. Papp, Ladislaus L. Torday, Gregory A. Chass, Joseph C.P Koo, András Varró

Publikováno v: Journal of Molecular Structure: THEOCHEM. 620:231-255

The sidechain conformational potential energy hypersurfaces (PEHS) for the γL, βL, αL, and αD backbone conformations of N-acetyl- l -aspartate-N′-methylamide were generated. Of the 81 possible conformers initially expected for the aspartate res

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3611cef528169004951001f2f72d5fab
https://doi.org/10.1016/s0166-1280(02)00639-5

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