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Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from Aspergillus
Abstract
X-ray diffraction analysis (at 2.1-A resolution) of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites. The primary site (which is essential in maintaining proper folding around the active site) contains a tightly bound Ca2+ with an unusually high number of eight ligands (O delta 1 and O delta 2 of Asp175, O delta of Asn121, main-chain carbonyl oxygens of Glu162 and Glu210, and three water molecules). A secondary binding site was identified at the bottom of the substrate binding cleft; it involves the residues presumed to play a catalytic role (Asp206 and Glu230). This explains the inhibitory effect of calcium observed at higher concentrations. Neutral Aspergillus oryzae (TAKA) alpha-amylase was also refined in a new crystal at 2.1-A resolution. The structure of this homologous (over 80%) enzyme and additional kinetic studies support all the structural conclusions regarding both calcium-binding sites.
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Cited by
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Davies, G., & Henrissat, B. (1995) · Structure · doi:10.1016/s0969-2126(01)00220-9 · Cited by 2,028
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D'Amico, S., Marx, J.-C., Gerday, C., & Feller, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212508200 · Cited by 455
The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes
Brayer, G. D., Luo, Y., & Withers, S. G. (1995) · Protein Science · doi:10.1002/pro.5560040908 · Cited by 408
Wallace, A. C., Borkakoti, N., & Thornton, J. M. (1997) · Protein Science · doi:10.1002/pro.5560061104 · Cited by 329
Reversible and irreversible unfolding of multi-domain proteins
Strucksberg, K. H., Rosenkranz, T., & Fitter, J. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.005 · Cited by 55
Metadata
- Authors
- Boel, E., Brady, L., Brzozowski, A. M., Derewenda, Z., Dodson, G. G., Jensen, V. J., Petersen, S. B., Swift, H., Thim, L., & Woldike, H. F.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-07-03
- Volume
- 29
- Issue
- 26
- Pages
- 6244-6249
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2101749711
- Cited by
- 316
- References
- 0
- FWCI
- 15.74
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from Aspergillus. https://app.cochat.ai/papers/10.1021/bi00478a019
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- Boel, E., Brady, L., Brzozowski, A. M., Derewenda, Z., Dodson, G. G., Jensen, V. J., Petersen, S. B., Swift, H., Thim, L., & Woldike, H. F. (1990). Calcium binding in .alpha.-amylases: an x-ray diffraction study at 2.1-.ANG. resolution of two enzymes from Aspergillus. Biochemistry. https://doi.org/10.1021/bi00478a019
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