The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase

Biological Chemistry

Volumn 386, Issue 8, 2005, Pages 791-799

  Dostál, Jiří ^a   Dlouhá, Helena ^a   Maloň, Petr ^a   Pichová, Iva ^a   Hrušková Heidingsfeldova, Olga ^a  

^a INSTITUTE OF ORGANIC CHEMISTRY AND BIOCHEMISTRY   (Czech Republic)

Author keywords

Aspartic proteinase; Candida parapsilosis; Circular dichroism; His6 tag; Zymogen conversion

Indexed keywords

ASPARTIC PROTEINASE; ENZYME PRECURSOR; MEMBRANE ENZYME; PROTEIN SAPP1P; PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; CANDIDA PARAPSILOSIS; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME SYNTHESIS; ESCHERICHIA COLI; FUNGAL CELL; GENE CONVERSION; GENETIC CODE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; BLOTTING, WESTERN; CANDIDA; CELL MEMBRANE; ENZYME PRECURSORS; GENES, FUNGAL; HISTIDINE; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROPROTEIN CONVERTASES; PROTEASE INHIBITORS; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY;

CANDIDA; CANDIDA PARAPSILOSIS;

EID: 26844575139     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.093     Document Type: Article

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