Literature summary for 3.2.1.96 extracted from

Masuda, A.; Xu, J.; Mitsudome, T.; Morokuma, D.; Mon, H.; Banno, Y.; Kusakabe, T.; Lee, J.
Improvement of endo-beta-N-acetylglucosaminidase H production using silkworm-baculovirus protein expression system (2015), J. Asia Pac. Entomol., 18, 175-180 .

No PubMed abstract available

Search for more literature for 3.2.1.96

Cloned(Commentary)

Cloned (Comment)	Organism
silkworm-baculovirus expression system	Streptomyces plicatus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces plicatus	P04067	-	-

Purification (Commentary)

Purification (Comment)	Organism
the non-secreted form of Endo H without a signal peptide is expressed and purified from silkworm fat body	Streptomyces plicatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ribonuclease B + H2O	the enzyme catalyzes cleavage between the GlcNAc residues of the chitobiose core of N-linked glycans, leaving one GlcNAc residues attached to asparagine. Endo H cleaves high mannose and hybrid, but not complex, N-linked oligosaccharides on glycoproteins	Streptomyces plicatus	?	-	?

Synonyms

Synonyms	Comment	Organism
Endo H	-	Streptomyces plicatus
endo-beta-N-acetylglucosaminidase H	-	Streptomyces plicatus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)