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Volumn 36, Issue 2, 2002, Pages 77-84
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An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: Efficient cleavage of substrates with basic amino acids at the P4 and P6 positions
a a a a a
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SUNTORY LTD
(Japan)
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Author keywords
Atrial natriuretic peptide; Denaturing conditions; Glucagon like peptide 1; Processing enzyme; Substrate specificity
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Indexed keywords
AMINO ACIDS;
BIOLOGICAL MEMBRANES;
BIOTECHNOLOGY;
MANURES;
PROTEINS;
UREA;
CLEAVAGE EFFICIENCY;
ESCHERICHIA COLI;
AMINO ACID;
ARGININE;
ATRIAL NATRIURETIC FACTOR;
GLUCAGON LIKE PEPTIDE;
GLUTAMIC ACID;
HYBRID PROTEIN;
PROTEIN OMPT;
PROTEINASE;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ARTICLE;
CHEMICAL BOND;
CONGESTIVE HEART FAILURE;
DRUG SYNTHESIS;
ENZYME ANALYSIS;
ESCHERICHIA COLI;
MICHAELIS CONSTANT;
PEPTIDE SYNTHESIS;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
AMINO ACIDS, BASIC;
ATRIAL NATRIURETIC FACTOR;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HUMANS;
KINETICS;
MEMBRANE PROTEINS;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE HYDROLASES;
PLASMIDS;
PORINS;
RECOMBINANT FUSION PROTEINS;
SENSITIVITY AND SPECIFICITY;
SPECIES SPECIFICITY;
SUBSTRATE SPECIFICITY;
ESCHERICHIA COLI;
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EID: 0036794384
PISSN: 08854513
EISSN: None
Source Type: Journal
DOI: 10.1042/BA20020037 Document Type: Article |
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Times cited : (10)
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References (32)
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