Literature summary extracted from

Sugawara, K.; Tajima, Y.; Kawashima, I.; Tsukimura, T.; Saito, S.; Ohno, K.; Iwamoto, K.; Kobayashi, T.; Itoh, K.; Sakuraba, H.
Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease (2009), Mol. Genet. Metab., 96, 233-238.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
3.2.1.22	1-deoxy-L-altronojirimycin hydrochloride	1000fold less effective than 1-deoxygalactonojirimycin	Homo sapiens
3.2.1.22	1-deoxygalactonojirimycin	binding to the enzyme protein is enthalpy-driven and stronger than binding of galactostatin bisulfite. Inhibitor fits to the active-site pocket and undergoes hydrogen bonding with residues comprising the active-site pocket including the catalytic ones	Homo sapiens
3.2.1.22	galactostatin bisulfite	inhibits in vitro, increases enzyme activity in cultured Fabry fibroblasts. Binding is less strong than binding of 1-deoxygalactonojirimycin, and interaction with enzyme protein is mainly enthalpie-driven but entropy-driven factors may be involved. Inhibitor fits to the active-site pocket and undergoes hydrogen bonding with residues comprising the active-site pocket including the catalytic ones	Homo sapiens
3.2.1.22	n-butyldeoxygalactonojirimycin	2000fold less effective than 1-deoxygalactonojirimycin	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.22	Homo sapiens	P06280	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3.2.1.22	4-methylumbelliferyl alpha-D-galactoside + H2O	-	Homo sapiens	4-methylumbelliferone + alpha-D-galactose	-	?

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)