Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 19, 2005, Pages 6855-6860

  Varadarajan, Navin ^a   Gam, Jongsik ^a   Olsen, Mark J ^a   Georgiou, George ^a,b   Iverson, Brent L ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^b The University of Texas at Austin   (United States)

Author keywords

Engineering; Flow cytometry

Indexed keywords

ALANINE; ARGININE; ENDOPEPTIDASE OMPT; ENZYME VARIANT; PROTEINASE; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME ENGINEERING; ENZYME ISOLATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; EVOLUTION; FLOW CYTOMETRY; GENETIC SELECTION; NONHUMAN; PRIORITY JOURNAL;

ARGININE; BIOCHEMISTRY; CATALYSIS; CELL SEPARATION; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; ENZYMES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLOW CYTOMETRY; GENE LIBRARY; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; PEPTIDE HYDROLASES; PEPTIDES; PORINS; PROTEIN BINDING; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 18744388856     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0500063102     Document Type: Article

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