pH Dependence of penicillin amidase enantioselectivity for charged substrates

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1433, Issue 1-2, 1999, Pages 327-334

  Lummer, Karsten ^a   Rieks, André ^a   Galunsky, Boris ^a   Kasche, Volker ^a  

^a HAMBURG UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Enantioselectivity; Enantioselectivity modulation; Penicillin amidase; pH dependence; Stereoselectivity

Indexed keywords

PENICILLIN AMIDASE;

ARTICLE; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PH; PRIORITY JOURNAL; STEREOCHEMISTRY; STEREOSPECIFICITY;

BINDING SITES; CATALYSIS; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; PENICILLIN AMIDASE; QUALITY CONTROL; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 0032797931     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00130-2     Document Type: Article

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