3.2.1.46: galactosylceramidase

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For detailed information about galactosylceramidase, go to the full flat file.

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Synonyms

beta-galactocerebrosidase, beta-galactosylceramidase, ceramidase, galacatosyl-, ceramide galactosidase, cerebroside beta-galactosidase, cerebroside galactosidase, galactoceramidase, galactocerebrosidase, galactocerebroside beta-galactosidase, galactocerebroside galactosidase, galactocerebroside-beta-D-galactosidase, Galactosylceramidase, galactosylceramidase I, galactosylceramide beta-galactosidase, galactosylcerebrosidase, GALC, galcerase, GM1 ganglioside beta-galactosidase, lactosylceramidase, lactosylceramidase I

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.46 galactosylceramidase

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Results	in table
15	Activating Compound
2042	AA Sequence
23	Application
1	CAS Registry Number
9	Cloned(Commentary)
1	Crystallization (Commentary)
1040	Disease/ Diagnostics
8	General Information
2	General Stability
22	Inhibitors
15	KM Value [mM]
9	Localization
1	Metals/Ions
19	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
39	Organism
2	Pathway
15	PDB ID
15	pH Optimum
5	pH Range
1	Posttranslational Modification
9	Protein Variants
11	Purification (Commentary)
1	Reaction
5	Reaction Type
38	Reference
55	Source Tissue
20	Specific Activity [micromol/min/mg]
99	Substrates and Products (Substrate)
4	Subunits
29	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
4	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.2.1.46 - galactosylceramidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structures of GALC and the GALC-D-galactose product complex, to 2.1 and 2.4 A resolution, respectively. The overall fold comprises a central triosephosphate isomerase barrel, a beta-sandwich domain, and a lectin domain. The overall fold of GALC is unchanged upon galactose binding, the core of the binding pocket being formed by the long loops on the C-terminal face of the TIM barrel. Loops from both the beta-sandwich and lectin domains also contribute to the substrate-binding pocket, and mutations involved in Krabbe's disease are widely distributed throughout the protein

Mus musculus

P54818

716780