[Structure and evolution of mammalian maltase-glucoamylase and sucrase-isomaltase genes].
Maltase-glucoamylase and sucrase-isomaltase are two human glycosidases responsible for starch digestion. We have performed a comparative analysis of their amino acid sequences from several species of mammals and their orthologues from other chordates. This allowed us to determine the evolutionary history of the enzymes. Both glycosidases are paralogues and contain GH31 family catalytic domains. The common evolutionary precursor of these genes has arisen by a tandem duplication. As a consequence, sucrase-isomaltase consists of two homologous parts. The maltase-glucoamylase gene was a subject of several additional duplications, which number was not the same in different mammals. The locus, containing this gene, consists of 4-7 tandem repeats. The amino acid sequence, encoded by each of them, is similar to both parts of sucrase-isomaltase.
Naumov
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D000818:Animals; D019143:Evolution, Molecular; D006801:Humans; D008322:Mammals; D010802:Phylogeny; D013394:Sucrase-Isomaltase Complex / Q000235:genetics*; D000520:alpha-Glucosidases / Q000235:genetics*
D013394:Sucrase-Isomaltase Complex; D000520:alpha-Glucosidases