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