Mutagenesis of the glucoamylase signal peptide of Saccharomyces diastaticus and functional analysis in Saccharomyces cerevisiae

FEMS Microbiology Letters

Volumn 193, Issue 1, 2000, Pages 7-11

  Lee, Jun Won ^a   Kang, Dae Ook ^a   Kim, Bo Yeon ^a   Oh, Won Keun ^a   Mheen, Tae Ick ^a   Pyun, Yu Ryang ^b   Ahn, Jong Seog ^a  

^a Daejin University   (South Korea)

^b Yonsei University   (South Korea)

Author keywords

Bacillus endo 1,4 D glucanase; Glucoamylase signal peptide; Mutagenesis; Saccharomyces cerevisiae; Saccharomyces diastaticus; Secretion

Indexed keywords

CELLULASE; GLUCAN 1,4 ALPHA GLUCOSIDASE; MUTANT PROTEIN; SIGNAL PEPTIDE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME RELEASE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECRETION; REPORTER GENE; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; BASE SEQUENCE; CELLULASE; GENES, REPORTER; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLYCOSIDE HYDROLASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN SORTING SIGNALS; RECOMBINANT PROTEINS; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; TRANSFORMATION, GENETIC;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE VAR. DIASTATICUS;

EID: 0034559738     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(00)00449-3     Document Type: Article

References (19)

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19. Important role of the proline residue in the signal sequence that directs the secretion of human lysozyme in Saccharomyces cerevisiae