alpha-galactosidase A (ceramide trihexosidase, melibiase, GLA)

Function: - hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans & galactohydrolase - catalyzes hydrolysis of melibiose into galactose & glucose Structure: - homodimer - belongs to the glycosyl hydrolase 27 family Compartment: lysosome RNA editing: modified positions=396; note=partially edited Pathology: - defects in GLA are the cause of Fabry disease Biotechnology: - used to convert blood group antigens of type B into type O, the universal donor type Pharmacology: - recombinant alpha-galactosidase A - available as agalsidase beta under the names - Replagal (Transkaryotic Therapies) - Fabrazyme (Genzyme) - available as pegunigalsidase alfa (Elfabrio) Genetics: Gene locus: Xq22 Laboratory: - GLA gene mutation - alpha-galactosidase A in fibroblasts - alpha-galactosidase A in leukocytes

Specific

agalsidase beta (Fabrazyme, Replagal) alpha-D-galactosidase enzyme (Beano) pegunigalsidase alfa-iwxj (Elfabrio)

General

alpha-galactosidase or galactoside galactohydrolase glycoprotein

Properties

SIZE: entity length = 429 aa MW = 49 kD COMPARTMENT: lysosome MOTIF: signal sequence {1-31} cysteine residue {C52} MODIFICATION: cysteine residue {C94} cysteine residue {C56} MODIFICATION: cysteine residue {C63} cysteine residue {C63} MODIFICATION: cysteine residue {C56} cysteine residue {C94} MODIFICATION: cysteine residue {C52} N-glycosylation site {N139} cysteine residue {C142} MODIFICATION: cysteine residue {C172} aspartate residue {D170} cysteine residue {C172} MODIFICATION: cysteine residue {C142} N-glycosylation site {N192} cysteine residue {C202} MODIFICATION: cysteine residue {C223} Substrate binding {203-207} N-glycosylation site {N215} cysteine residue {C223} MODIFICATION: cysteine residue {C202} aspartate residue {D231} cysteine residue {C378} MODIFICATION: cysteine residue {C382} cysteine residue {C382} MODIFICATION: cysteine residue {C378} N-glycosylation site {N408}

Database Correlations

OMIM 301500 UniProt P06280 Pfam PF02065 Entrez Gene 2717 ENZYME 3.2.1.22