Literature summary for 3.2.1.45 extracted from

Premkumar, L.; Sawkar, A.R.; Boldin-Adamsky, S.; Toker, L.; Silman, I.; Kelly, J.W.; Futerman, A.H.; Sussman, J.L.
X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide: implications for Gaucher disease (2005), J. Biol. Chem., 280, 23815-23819.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N396T	mutation causing Gaucher disease, mutation stabilizes closed conformation and destabilizes open conformation of the enzyme, thus limiting substrate access to the active site	Homo sapiens
R395P	mutation causing Gaucher disease, destabilizes the open conformation of the enzyme due to the loss of a stabilizing salt bridge with Glu388, thus limiting substrate access to the active site	Homo sapiens
V394L	mutation causing Gaucher disease, mutation stabilizes closed conformation and destabilizes open conformation of the enzyme, thus limiting substrate access to the active site	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
conduritol-B-epoxide	irreversible	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P04062	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-(6-(7-nitrobenzo-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-D-erythro-glucosylsphingosine + H2O	-	Homo sapiens	D-glucose + N-(6-(7-nitrobenzo-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-sphingosine	-	?

Synonyms

Synonyms	Comment	Organism
Cerezyme	-	Homo sapiens
GlcCerase	-	Homo sapiens

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Release 2023.1 (January 2023)