Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.

@article{Valle1998BarleyAB,
  title={Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.},
  author={Franck Vall{\'e}e and Anders Kadziola and Yves Bourne and Michel Juy and Kees W Rodenburg and Birte Svensson and Richard Haser},
  journal={Structure},
  year={1998},
  volume={6 5},
  pages={649-59}
}
BACKGROUND Barley alpha-amylase is a 45 kDa enzyme which is involved in starch degradation during barley seed germination. The released sugars provide the plant embryo with energy for growth. The major barley alpha-amylase isozyme (AMY2) binds with high affinity to the endogenous inhibitor BASI (barley alpha-amylase/subtilisin inhibitor) whereas the minor isozyme (AMY1) is not inhibited. BASI is a 19.6 kDa bifunctional protein that can simultaneously inhibit AMY2 and serine proteases of the… CONTINUE READING