title: Secretion of psychrophilic alpha-amylase deletion mutants in Pseudoalteromonas haloplanktis TAC125.
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.
authors.affiliation: Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario M.S. Angelo via Cynthia, Napoli Italia.
authors.forename: Angela Maria
authors.initials: AM
authors.lastname: Cusano
authors.forename: Ermenegilda
authors.initials: E
authors.lastname: Parrilli
authors.forename: Angela
authors.initials: A
authors.lastname: Duilio
authors.forename: Giovanni
authors.initials: G
authors.lastname: Sannia
authors.forename: Gennaro
authors.initials: G
authors.lastname: Marino
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Tutino
mesh_terms: D009154:Mutation; D010957:Plasmids; D031161:Pseudoalteromonas / Q000201:enzymology* / Q000235:genetics; D000516:alpha-Amylases / Q000378:metabolism*; D001618:beta-Lactamases / Q000502:physiology
chemical_list: D000516:alpha-Amylases; D001618:beta-Lactamases