Literature summary for 3.5.1.52 extracted from

Suzuki, T.; Kitajima, K.; Inoue, Y.; Inoue, S.
Carbohydrate-binding property of peptide:N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides (1995), J. Biol. Chem., 270, 15181-15186.

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Inhibitors

Inhibitors	Comment	Organism	Structure
N,N'-diacetylchitobiose	-	Elizabethkingia meningoseptica
N,N'-diacetylchitobiose	GlcNAc2, competitive inhibitor may be directly accessible to the catalytic site	Mus musculus
N,N'-diacetylchitobiose	-	Prunus amygdalus var. dulcis
N-ethylmaleimide	2 mM, significant inhibition by thiol-modification, alkylation	Mus musculus
triomannose	evidence for occupation of the carbohydrate-binding site	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Elizabethkingia meningoseptica	-	-	-
Mus musculus	-	-	-
Prunus amygdalus var. dulcis	-	almond	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mus musculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
fibroblast	C3H mouse-derived L-929 fibroblast cells	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
bovine fetuin glycopeptide + H2O	Leu-Asn(Man3Gal3GlcNAc5)-Asp-Ser-Arg	Mus musculus	?	-	?
additional information	-	Mus musculus	?	-	?
additional information	-	Prunus amygdalus var. dulcis	?	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Mus musculus
dimer	-	Prunus amygdalus var. dulcis

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Release 2023.1 (January 2023)