It has been shown [1,2,3,E1] that the following glycosyl hydrolases can be, on
the basis of sequence similarities, classified into a single family:
Lysosomal α-glucosidase (EC 3.2.1.20) (acid maltase) is a vertebrate
glycosidase active at low pH, which hydrolyzes α(1->4) and α(1->6)
linkages in glycogen, maltose, and isomaltose.
α-glucosidase (EC 3.2.1.20) from the yeast Candida tsukunbaensis.
α-glucosidase (EC 3.2.1.20) (gene malA) from the archebacteria
Sulfolobus solfataricus.
Intestinal sucrase-isomaltase (EC 3.2.1.48 / EC 3.2.1.10) is a vertebrate
membrane-bound, multifunctional enzyme complex which hydrolyzes sucrose,
maltose and isomaltose. The sucrase and isomaltase domains of the enzyme
are homologous (41% of amino acid identity) and have most probably evolved
by duplication.
Glucoamylase 1 (EC 3.2.1.3) (glucan 1,4-α-glucosidase) from various
fungal species.
Yeast hypothetical protein YBR229c.
Fission yeast hypothetical protein SpAC30D11.01c.
An aspartic acid has been implicated [4] in the catalytic activity of sucrase,
isomaltase, and lysosomal α-glucosidase. The region around this active
residue is highly conserved and can be used as a signature pattern. We have
used a second region, which contains two conserved cysteines, as an additional
signature pattern.
Primary structure and processing of the Candida tsukubaensis alpha-glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex and human lysosomal alpha-glucosidase.
Naim H.Y. Niermann T. Kleinhans U. Hollenberg C.P. Strasser A.W.M.
Title
Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene.
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