| Literature DB >> 16630257 |
Angela Maria Cusano1, Ermenegilda Parrilli, Angela Duilio, Giovanni Sannia, Gennaro Marino, Maria Luisa Tutino.
Abstract
The nature and location of structural features responsible for the secretion of a cold-adapted alpha-amylase in the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 was studied by deletion mutagenesis of the wild-type enzyme and of chimerical proteins derived from the fusion of the alpha-amylase with a reporter enzyme. Domain C of the psychrophilic alpha-amylase contains secretion features involved in extracellular targeting.Entities:
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Year: 2006 PMID: 16630257 DOI: 10.1111/j.1574-6968.2006.00193.x
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742