Journal
BIOINFORMATICS
Volume 18, Issue 11, Pages 1534-1537Publisher
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/18.11.1534
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The sequence of the starch-binding domain present in 10% of amylolytic enzymes of microbial origin and classified as the carbohydrate-binding module family 20, was identified in the equivalent part of sequence of human genethonin, a skeletal muscle protein of unknown function. The sequence identity between the starch-binding domain from Bacillus sp. strain 1011 cyclodextrin glucanotransferase and the corresponding segment of human genethonin was higher than 28%. The amino acid residues known to be involved in the raw starch binding were found to be conserved in the genethonin sequence. The three-dimensional structure of the genethonin 'starch-binding domain' was modelled and its eventual function briefly discussed.
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