Relationship of sequence and structure to specificity in the α-amylase family of enzymes

By E. Macgregor, Š. Janeček, B. Svensson. 2001

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Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica (2005, background): “All proteins belonging to the a-amylase family have four conserved regions (see MacGregor et al. 2001), three of which contain the active site residues: two aspartate residues in boxes II and IV respectively, and a glutamate in box III.”
Microbial α-amylases: a biotechnological perspective (2003, background): “Structural conformation plays an important role on amylase activity [151].”
Understanding the effects of diet on bacterial metabolism in the large intestine (2007, background): “Starch-degrading enzymes are grouped into different families depending on their structure (MacGregor et al. 2001, http://afmb. cnrs-mrs.fr/CAZY/) and include a-amylases that hydrolyse a-1,4- linkages, type I pullulanases that specifically cleave a-1,6- bonds and amylopullulanases that possess both…”