The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation
Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G. (2003). The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation. Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2): 119-122. https://dx.doi.org/10.1016/S1570-9639(03)00184-5
In: Biochimica et Biophysica Acta-Proteins and Proteomics. ELSEVIER SCIENCE BV: Amsterdam. ISSN 1570-9639; e-ISSN 0006-3002, meer
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| Author keywords |
alpha-amylase; psychrophile; autotransporter; microcalorimetry; infraredspectroscopy |
| Auteurs | | Top |
- Claverie, P.
- Vigano, C.
- Ruysschaert, J.-M.
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| Abstract |
The α-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted β-barrel of autotransporters, this C-terminal propeptide displays a noticeable α-helix content. It is connected to the enzyme by a disordered linker and has no significant interaction with the catalytic domain. The microcalorimetric pattern of the precursor also demonstrates that the stability of protein domains may evolve differently. |
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