A Novel Homozygous Variant in the Aspartoacylase Gene Causes Canavan Disease-Case Report

Autor:	Archana Vaddinahalli Kariyappa, Shilpa Krishnapura Lakshminarayana, Dhanalakshmi Kumble, Kavitha Siddappa, Kalpana Ramesh Yelsangikar, Mallesh Kariyappa, Thotakura Pranga Lakshmi, Ashwin Dalal
Jazyk:	English<br />Turkish
Rok vydání:	2024
Předmět:	aspartoacylase brain canavan disease mutation myelin n-acetylaspartate Medicine Pediatrics RJ1-570
Zdroj:	Journal of Pediatric Research, Vol 11, Iss 4, Pp 250-253 (2024)
Druh dokumentu:	article
ISSN:	2147-9445 2587-2478
DOI:	10.4274/jpr.galenos.2024.55706
Popis:	Glu178 is the active site residue essential for substrate affinity and catalytic activity of the aspartoacylase enzyme. Sanger sequencing in an infant with Canavan disease revealed a homozygous ASPA: c.532G>A: p. (Glu178Lys) variant. Glu178Lys is the first ever variant reported at the critical active site of aspartoacylase protein and this variant might significantly disrupt substrate interaction.
Databáze:	Directory of Open Access Journals
Externí odkaz:	https://doaj.org/article/c12e573786e44486b5ffb1e04e736932 Zobrazit plný text záznamu View record in DOAJ Plný text ve formátu PDF Plný text ve formátu HTML
Nepřihlášeným uživatelům se plný text nezobrazuje	K zobrazení výsledku je třeba se přihlásit.