Literature summary for 3.2.1.207 extracted from

Olson, L.; Orsi, R.; Peterson, F.; Parodi, A.; Kim, J.; DAlessio, C.; Dahms, N.
Crystal structure and functional analyses of the lectin domain of glucosidase II insights into oligomannose recognition (2015), Biochemistry, 54, 4097-4111 .

Search for more literature for 3.2.1.207

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Schizosaccharomyces pombe

Crystallization (Commentary)

Crystallization (Comment)	Organism
mannose 6-phosphate receptor homology domain of GII beta subunit bound to mannose, to 1.6 A resolution. No major difference in the overall fold of ligand-bound and unbound structures, but a repositioning of side chains throughout the binding pocket, including Y372	Schizosaccharomyces pombe

Protein Variants

Protein Variants	Comment	Organism
additional information	mutations of the primary binding pocket residues and adjacent W409, all inhibit the activity of GII both in vitro and in vivo, they do not cause a significant change in the overall fold of the GII beta subunit mannose 6-phosphate receptor homology domain but impact locally the stability of the binding pocket	Schizosaccharomyces pombe
W409A	mutation substantially decreases GII activity	Schizosaccharomyces pombe
Y372A	mutation of Y372 substantially decreases GII activity	Schizosaccharomyces pombe
Y372F	mutation of Y372 substantially decreases GII activity	Schizosaccharomyces pombe

Organism

Organism	UniProt	Comment	Textmining
Schizosaccharomyces pombe	Q9USH8	glucosidase 2 subunit beta	-
Schizosaccharomyces pombe 972	Q9USH8	glucosidase 2 subunit beta	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GlcMan9GlcNAc + H2O	-	Schizosaccharomyces pombe	D-glucose + Man9GlcNAc	-	?
GlcMan9GlcNAc + H2O	-	Schizosaccharomyces pombe 972	D-glucose + Man9GlcNAc	-	?

Synonyms

Synonyms	Comment	Organism
GTB1	-	Schizosaccharomyces pombe

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)