Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding

Biochemical Journal

Volumn 371, Issue 1, 2003, Pages 143-150

  Morillas, Manuel ^a,d   McVey, Colin E ^b,e   Brannigan, James A ^b   Ladurner, Andreas G ^b,f   Forney, Larry J ^c   Virden, Richard ^a  

^a NEWCASTLE UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF YORK   (United Kingdom)

^c UNIVERSITY OF IDAHO   (United States)

^d ETH ZURICH   (Switzerland)

^e IMPERIAL COLLEGE LONDON   (United Kingdom)

^f UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Directed evolution; Enzyme kinetics; Three dimensional structure

Indexed keywords

CATALYST ACTIVITY; CRYSTAL STRUCTURE; ENTROPY; PROTEINS; SUBSTRATES;

HEAT INACTIVATION;

BIOCHEMISTRY;

AMIDASE; CYSTEINE; GLUTARYLLEUCINE; LEUCINE; MUTANT PROTEIN; PENICILLIN ACYLASE; PHENYLALANINE; UNCLASSIFIED DRUG; UREA; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; GLUTARIC ACID DERIVATIVE; PENICILLIN AMIDASE;

AMINO ACID ANALYSIS; ARTICLE; BACTERIAL STRAIN; BETA CHAIN; BINDING AFFINITY; CATALYSIS; CODON; CONFORMATION; CRYSTAL STRUCTURE; DENATURATION; ENTROPY; ENZYME SPECIFICITY; ESCHERICHIA COLI; FLUORESCENCE; MOLECULAR MODEL; MONITORING; MUTATION; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; ROTATION; WILD TYPE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN DENATURATION; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GLUTARATES; KINETICS; LEUCINE; MODELS, MOLECULAR; MUTATION; PENICILLIN AMIDASE; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; SUBSTRATE SPECIFICITY; UREA;

EID: 0242286152     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021383     Document Type: Article

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