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The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation

✍ Scribed by Paule Claverie; Catherine Vigano; Jean-Marie Ruysschaert; Charles Gerday; Georges Feller

Publisher
Elsevier Science
Year
2003
Tongue
English
Weight
152 KB
Volume
1649
Category
Article
ISSN
1570-9639

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✦ Synopsis

The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted beta-barrel of autotransporters, this C-terminal propeptide displays a noticeable alpha-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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