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3.2.1.45: glucosylceramidase

This is an abbreviated version!
For detailed information about glucosylceramidase, go to the full flat file.

Word Map on EC 3.2.1.45

Reaction

a D-glucosyl-N-acylsphingosine
+
H2O
=
D-glucose
+
a ceramide

Synonyms

ABG, acid beta-D-glucosidase, acid beta-glucocerebrosidase, acid beta-glucosidase, acid beta-glucosylceramidase, acid beta-glycosidase, acid glucosylceramidase, acid-beta-glucocerebrosidase, acid-beta-glucosidase, Alglucerase, beta-D-glucocerebrosidase, beta-GC, beta-glucocerebrosidase, beta-glucosidase, beta-glucosidase 2, beta-glucosylceramidase, beta-glucosylceramidase 2, beta-glycosylceramidase, bile acid beta-glucosidase, ceramidase, glucosyl-, ceramide glucosidase, cerebroside beta-glucosidase, Ceredase, Cerezyme, D-glucosyl-N-acylsphingosine glucohydrolase, GBA, GBA1, GBA2, Gcase, GCD, GCR, GDA, gene-activated human GlcCerase, Glc-Cerase, glcCer-beta-glucosidase, GlcCerase, glucocerebrosidase, glucocerebroside beta-glucosidase, glucose cerebrosidase, glucosphingosine glucosylhydrolase, glucosylceramidase, glucosylceramide beta-glucosidase, glucosylcerebrosidase, glucosylsphingosine beta-D-glucosidase, glucosylsphingosine beta-glucosidase, glycosylceramidase, glycosylceramide-beta-glucosidase, Imiglucerase, Klotho-related protein, KLrP, lysosomal glucosylceramidase, microsomal bile acid beta-glucosidase, N-acylsphingosyl-1-O-beta-D-glucoside:glucohydrolase, neutral beta-glycosylceramidase, neutral glucosylceramidase, NLGase, non-lysosomal beta-glucosylceramidase, non-lysosomal glucosylceramidase, nonlysosomal beta-glucosidase, nonlysosomal glucosylceramidase, psychosine hydrolase, taliglucerase alfa, velaglucerase alfa, Vpriv

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.45 glucosylceramidase

Oxidation Stability

Oxidation Stability on EC 3.2.1.45 - glucosylceramidase

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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
forced oxidation of GCase that results in a 40-60% reduction in in vitro biological activity affects the stability of some key structural elements within the catalytic site. These changes in dynamics occur on a longer time scale that is irrelevant for catalysis, effectively ruling out loss of structure in the catalytic site as a major factor contributing to the reduction of the catalytic activity. Oxidation also leads to noticeable destabilization of conformation in remote protein segments on a much larger scale, which is likely to increase the aggregation propensity of GCase and affect its bioavailability
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