Title : Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity.

Pub. Date : 2008 Mar 18

PMID : 18284212






3 Functional Relationships(s)
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1 To probe the role such interactions play in allosteric activation, further structural analyses were conducted in the presence of acarbose, which served as a sensitive reporter molecule of the catalytic ability of these modified enzymes to carry out its expected rearrangement by human pancreatic alpha-amylase. Acarbose amylase alpha 2A Homo sapiens
2 In contrast, while nitrite considerably boosts the relative activity of human pancreatic alpha-amylase, its presence leads to changes in the electrostatic environment and active site conformations that substantially modify catalytic parameters and produce a novel acarbose rearrangement product. Acarbose amylase alpha 2A Homo sapiens
3 In particular, nitrite-substituted human pancreatic alpha-amylase demonstrates the unique ability to cleave acarbose into its acarviosine and maltose parts and carry out a previously unseen product elongation. Acarbose amylase alpha 2A Homo sapiens