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Striking structural and functional similarities suggest that intestinal sucrase‐isomaltase, human lysosomal α‐glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene
Author(s) -
Naim Hassan Y.,
Niermann Thomas,
Kleinhans Ulrich,
Hollenberg Cornelis P.,
Strasser Alexander W.M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81353-a
Subject(s) - gene , genetics , biology , sucrase , biochemistry , enzyme
Sequence comparison of the primary structure of the yeast Schwanniomyces occidentalis glucoamylase (GAM) with GAMs in different microorganisms did not reveal significant similarities. By contrast, striking similarities were, surprisingly, found with 3 mammalian secretory and integral membrane proteins: the 2 subunits of intestinal brush border sucrase‐isomaltase and human lysosomal α‐glucosidase. The similarities among these proteins are found as clusters of up to 8 amino acids and distributed all over the protein sequences. The major sequence differences are found in the N‐terminal regions accounting, probably, for the different cellular locations of these proteins. The high level of similarities between sucrase, isomaltase, Sch. occidentalis GAM and human lysosomal α‐glucosidase suggest that these proteins are derived from the same ancestral gene. To our knowledge, this is the first report that describes similarities between a yeast secretory protein and mammalian secretory and integral membrane proteins.