Literature summary for 2.4.99.21 extracted from

Matsumoto, S.; Taguchi, Y.; Shimada, A.; Igura, M.; Kohda, D.
Tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex (2017), Biochemistry, 56, 602-611 .

Search for more literature for 2.4.99.21

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method of G617C mutant protein, the crystal structure of the cross-linked AfAglB-peptide complex is determined to 3.5 A resolution	Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	O29867	-	-
Archaeoglobus fulgidus ATCC 49558	O29867	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex	Archaeoglobus fulgidus	?	-	-
additional information	tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex	Archaeoglobus fulgidus ATCC 49558	?	-	-

Synonyms

Synonyms	Comment	Organism
AglB	-	Archaeoglobus fulgidus

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Release 2023.1 (January 2023)