A tryptophan residue is identified in the substrate binding of penicillin G acylase from Kluyvera citrophila

Enzyme and Microbial Technology

Volumn 40, Issue 5, 2007, Pages 1389-1397

  Kumar, R Suresh ^a   Prabhune, A A ^a   Pundle, A V ^a   Karthikeyan, M ^a   Suresh, C G ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

Fluorescence measurement; K. citrophila; Penicillin G acylase; Sequence alignment; Substrate docking; Tryptophan modification

Indexed keywords

FLUORESCENCE MEASUREMENT; K. CITROPHILA; PENICILLIN G ACYLASE; SEQUENCE ALIGNMENT; SUBSTRATE DOCKING; TRYPTOPHAN MODIFICATION;

ANTIBIOTICS; CHEMICAL MODIFICATION; ENZYME KINETICS; FLUORESCENCE;

AMINO ACIDS;

2 HYDROXY 5 NITROBENZYL BROMIDE; 6 AMINOPENICILLANIC ACID; AMIDASE; BETA LACTAM ANTIBIOTIC; N BROMOSUCCINAMIDE; PENICILLIN G ACYLASE; REAGENT; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; DRUG INDUSTRY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME PURIFICATION; ENZYME SUBSTRATE; FLUORESCENCE; KLUYVERA CRYOCRESCENS; NONHUMAN; PHOTOCHEMICAL QUENCHING; PROTEIN MODIFICATION; STRUCTURE ANALYSIS; TRYPTOPHAN METABOLISM;

KLUYVERA CRYOCRESCENS;

EID: 33847637189     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.10.022     Document Type: Article

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