The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation.
Biochim Biophys Acta
; 1649(2): 119-22, 2003 Jul 30.
Article
em En
| MEDLINE
| ID: mdl-12878029
ABSTRACT
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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Base de dados:
MEDLINE
Assunto principal:
Precursores de Proteínas
/
Temperatura Baixa
/
Pseudoalteromonas
/
Alfa-Amilases
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article