Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius

Autor(en): Herrmann, A
Schlosser, A
Schmid, R
Schneider, E 
Stichwörter: Alicyclobacillus acidocaldarius; AMYLASE; BACILLUS-ACIDOCALDARIUS; binding protein-dependent transport system; ESCHERICHIA-COLI; Gram(+) bacteria; maltose; maltose uptake; Microbiology; PROTEIN; thermoacidophile; TRANSPORT
Erscheinungsdatum: 1996
Herausgeber: EDITIONS SCIENTIFIQUES ELSEVIER
Journal: RESEARCH IN MICROBIOLOGY
Volumen: 147
Ausgabe: 9
Startseite: 733
Seitenende: 737
Zusammenfassung: 
Growth of the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius strain ATCC 27009 on maltose resulted in the increased production of a protein with apparent molecular mass of 40 kDa. By metabolic labelling with C-14-palmitic acid, the 40-kDa protein was identified as a lipoprotein. The protein exhibited maltose-binding activity at pH 3.5, as demonstrated by chromatography on cross-linked amylose. Partial amino acid sequence analysis revealed that the 40-kDa protein coresponds to the product of an open reading frame downstream from the amylase gene (amy) that displays similarity to enterobacterial maltose-binding proteins.
ISSN: 09232508
DOI: 10.1016/S0923-2508(97)85120-0

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