Identification of residues for chaperone-like activity of OppA protein in Yersinia pseudotuberculosis

Autor:	Elena Escobar Garduño, Thomas Scior, Lucia Soto Urzúa, Luis Javier Martínez Morales
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	α-glucosidase Lactate dehydrogenase OppA Site-directed mutagenesis Analogy modeling Chaperone-like activity Biotechnology TP248.13-248.65 Microbiology QR1-502
Zdroj:	AMB Express, Vol 10, Iss 1, Pp 1-10 (2020)
Druh dokumentu:	article
ISSN:	2191-0855
DOI:	10.1186/s13568-020-01090-8
Popis:	Abstract Periplasmic oligopeptide binding protein (OppA) is part of a multimeric cytoplasmic membrane protein complex, whose function is known as peptide transporters found in Gram-negative bacteria. A chaperone-like activity has been found for the OppA from Yersinia pseudotuberculosis, using biochemical experiments. Through computational analysis, we selected two amino acid residues (R41 and D42) that probably are involved in the chaperone-like activity. Our results to corroborate how OppA assists refolding and renaturation of lactate dehydrogenase and alpha-glucosidase denatured enzymes.
Databáze:	Directory of Open Access Journals
Externí odkaz:	https://doaj.org/article/9a5e316b728a471db450628656be479e Zobrazit plný text záznamu View record in DOAJ Plný text ve formátu PDF Plný text ve formátu HTML
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