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A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.

Strobl S, Maskos K, Wiegand G, Huber R, Gomis-Rüth FX, Glockshuber R
Structure 6 911-21 (1998)
Cited: 81 times
EuropePMC logo PMID: 9687373

Abstract

Background

alpha-Amylases catalyze the hydrolysis of alpha-D-(1,4)-glucan linkages in starch and related compounds. There is a wide range of industrial and medical applications for these enzymes and their inhibitors. The Ragi bifunctional alpha-amylase/trypsin inhibitor (RBI) is the prototype of the cereal inhibitor superfamily and is the only member of this family that inhibits both trypsin and alpha-amylases. The mode of inhibition of alpha-amylases by these cereal inhibitors has so far been unknown.

Results

The crystal structure of yellow meal worm alpha-amylase (TMA) in complex with RBI was determined at 2.5 A resolution. RBI almost completely fills the substrate-binding site of TMA. Specifically, the free N terminus and the first residue (Ser1) of RBI interact with all three acidic residues of the active site of TMA (Asp185, Glu222 and Asp287). The complex is further stabilized by extensive interactions between the enzyme and inhibitor. Although there is no significant structural reorientation in TMA upon inhibitor binding, the N-terminal segment of RBI, which is highly flexible in the free inhibitor, adopts a 3(10)-helical conformation in the complex. RBI's trypsin-binding loop is located opposite the alpha-amylase-binding site, allowing simultaneous binding of alpha-amylase and trypsin.

Conclusion

The binding of RBI to TMA constitutes a new inhibition mechanism for alpha-amylases and should be general for all alpha-amylase inhibitors of the cereal inhibitor superfamily. Because RBI inhibits two important digestive enzymes of animals, it constitutes an efficient plant defense protein and may be used to protect crop plants from predatory insects.

Reviews - 1tmq mentioned but not cited (1)

  1. Structure, Function and Protein Engineering of Cereal-Type Inhibitors Acting on Amylolytic Enzymes. Møller MS, Svensson B. Front Mol Biosci 9 868568 (2022)

Articles - 1tmq mentioned but not cited (28)

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Reviews citing this publication (9)

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Related citations provided by authors (1)

  1. The Alpha-Amylase from the Yellow Meal Worm: Complete Primary Structure, Crystallization and Preliminary X-Ray Analysis. Strobl S, Gomis-Ruth FX, Maskos K, Frank G, Huber R, Glockshuber R FEBS Lett. 409 109-114 (1997)

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