Literature summary for 3.2.1.22 extracted from

Sugawara, K.; Ohno, K.; Saito, S.; Sakuraba, H.
Structural characterization of mutant alpha-galactosidases causing Fabry disease (2008), J. Hum. Genet., 53, 812-824.

Crystallization (Commentary)

Crystallization (Comment)	Organism
construction of structural models of mutant enzyme responsible for Fabry disease and calculation of indexes. Structural changes in the classic Fabry disease group are generally large and tend to be in the core region of a protein or located in the functionally important region, including the active-site pocket. Structural changes in the variant Fabry disease group are small or localized on the surface of the molecule far away from the activte site. Structural changes due to amino acid substitutions for which substrate analogues are effective for improving the stability or transportation are small or localized on the molecular surface	Homo sapiens

Crystallization (Comment)

Organism

construction of structural models of mutant enzyme responsible for Fabry disease and calculation of indexes. Structural changes in the classic Fabry disease group are generally large and tend to be in the core region of a protein or located in the functionally important region, including the active-site pocket. Structural changes in the variant Fabry disease group are small or localized on the surface of the molecule far away from the activte site. Structural changes due to amino acid substitutions for which substrate analogues are effective for improving the stability or transportation are small or localized on the molecular surface

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)