BOSTON—Calling itself “just a catalyst, nothing more,” humbled enzyme α-amylase confirmed Monday that while its contributions to a recent biochemical reaction significantly sped up the breakdown of starch into maltose, the formation of the disaccharide was, overall, a team effort. “All I did was lower the activation energy required for the reaction to take place, but if I don’t have an amazing substrate like starch to act upon, there is no reaction, period,” said the modest catabolic enzyme, adding that it’s easy to forget about the calcium ion, chloride ion, and the 496 amino-acid residues that all need to come together to make this biomolecule possible. “Say the pH isn’t slightly acidic, or say there is just one less carbon atom. Are we left with a simple sugar that can be used as an immediate energy source? Absolutely not. You need teamwork for that, and thankfully, that’s what we had today.” The reserved molecule added that, when it comes down to it, every atomic particle down to the very last electron owes the successful creation of maltose to a working pancreas.

Advertisement