Engineering of peptide synthetases. Key role of the thioesterase-like domain for efficient production of recombinant peptides

Journal of Biological Chemistry

Volumn 272, Issue 40, 1997, Pages 25304-25309

  De Ferra, Francesca ^a   Rodriguez, Francesco ^a   Tortora, Ornella ^a   Tosi, Claudio ^a   Grandi, Guido ^a,b  

^a Eniricerche SpA   (Italy)

^b Biocine SpA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PEPTIDE SYNTHASE; RECOMBINANT PROTEIN; THIOL ESTER HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENETIC ENGINEERING; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; BACTERIA; BACTERIAL PROTEINS; BASE SEQUENCE; BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; DNA PRIMERS; MOLECULAR SEQUENCE DATA; PEPTIDE SYNTHASES; PLASMIDS; PROTEIN ENGINEERING; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; THIOLESTER HYDROLASES;

BACILLUS SUBTILIS; FUNGI;

EID: 0030798978     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.40.25304     Document Type: Article

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