Literature summary for 2.6.1.16 extracted from

Chen, Q.; Mueller, J.S.; Pang, P.C.; Laval, S.H.; Haslam, S.M.; Lochmueller, H.; Dell, A.
Global N-linked glycosylation is not significantly impaired in myoblasts in congenital myasthenic syndromes caused by defective glutamine-fructose-6-phosphate transaminase 1 (GFPT1) (2015), Biomolecules, 5, 2758-2781.

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Application

Application	Comment	Organism
medicine	GFPT1 mutations in congenital myasthenic syndrome patients do not appear to compromise global N-glycosylation in muscle cells. The N-glycomes of myoblasts and myotubes derived from healthy controls, GFPT1 patients, and patients with other muscular diesease exhibit broadly similar levels of branching and relative abundances of bi-, tri-, and tetra-antennary N-glycans. Although some differences are observed in the relative abundances of some of the N-glycan constituents, these variations are modest and are not confined to the GFPT1 samples	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q06210	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
myoblast	-	Homo sapiens	-
myotube	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
GFPT1	-	Homo sapiens
glutamine-fructose-6-phosphate transaminase 1	-	Homo sapiens

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Release 2023.1 (January 2023)