Literature summary for 3.2.1.96 extracted from

Kitajima, T.; Jia, Y.; Komatsuzaki, A.; Cui, J.; Matsuzawa, F.; Aikawa, S.I.; Gao, X.D.; Chiba, Y.
Structural modeling and mutagenesis of endo-beta-N-acetylglucosaminidase from Ogataea minuta identifies the importance of Trp295 for hydrolytic activity (2018), J. Biosci. Bioeng., 125, 168-174 .

Search for more literature for 3.2.1.96

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Ogataea minuta

Protein Variants

Protein Variants	Comment	Organism
W295A	no endo-beta-N-acetylglucosaminidase activity	Ogataea minuta
W295E	no endo-beta-N-acetylglucosaminidase activity	Ogataea minuta
W295F	increased activity toward the agalacto-biantennary oligosaccharide compared with the wild-type enzyme, but decreased activities toward the trimannosyl core and high-mannose oligosaccharides	Ogataea minuta
W295Y	increased endo-beta-N-acetylglucosaminidase activity	Ogataea minuta

Organism

Organism	UniProt	Comment	Textmining
Ogataea minuta	R4WHQ8	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Ogataea minuta

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme has dual catalytic activity in the hydrolysis and transglycosylation of complex N-glycans. Trp295 is involved in the recognition of oligosaccharide substrates	Ogataea minuta	?	-	?

Synonyms

Synonyms	Comment	Organism
endo-beta-N-acetylglucosaminidase	-	Ogataea minuta
Endo-Om	-	Ogataea minuta

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Release 2023.1 (January 2023)