Abstract
A cold-active alpha-amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 degrees C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold-adapted enzyme have been initiated because a three-dimensional structure of a mesophilic counterpart, pig pancreatic alpha-amylase, already exists. alpha-Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic alpha-amylase, has been crystallized and data to 1.85 A have been collected. The space group is found to be C222(1) with a = 71.40 A, b = 138.88 A, and c = 115.66 A. Until now, a three-dimensional structure of a psychrophilic enzyme is lacking.
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Selected References
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- Arakawa T., Bhat R., Timasheff S. N. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry. 1990 Feb 20;29(7):1924–1931. doi: 10.1021/bi00459a037. [DOI] [PubMed] [Google Scholar]
- Arakawa T., Timasheff S. N. Theory of protein solubility. Methods Enzymol. 1985;114:49–77. doi: 10.1016/0076-6879(85)14005-x. [DOI] [PubMed] [Google Scholar]
- Brayer G. D., Luo Y., Withers S. G. The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Protein Sci. 1995 Sep;4(9):1730–1742. doi: 10.1002/pro.5560040908. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feller G., Lonhienne T., Deroanne C., Libioulle C., Van Beeumen J., Gerday C. Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J Biol Chem. 1992 Mar 15;267(8):5217–5221. [PubMed] [Google Scholar]
- Feller G., Payan F., Theys F., Qian M., Haser R., Gerday C. Stability and structural analysis of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem. 1994 Jun 1;222(2):441–447. doi: 10.1111/j.1432-1033.1994.tb18883.x. [DOI] [PubMed] [Google Scholar]
- Matthews B. W. Solvent content of protein crystals. J Mol Biol. 1968 Apr 28;33(2):491–497. doi: 10.1016/0022-2836(68)90205-2. [DOI] [PubMed] [Google Scholar]
- Qian M., Haser R., Payan F. Structure and molecular model refinement of pig pancreatic alpha-amylase at 2.1 A resolution. J Mol Biol. 1993 Jun 5;231(3):785–799. doi: 10.1006/jmbi.1993.1326. [DOI] [PubMed] [Google Scholar]