Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft

Journal of Molecular Biology

Volumn 302, Issue 4, 2000, Pages 887-898

  Hewitt, L ^a   Kasche, V ^b   Lummer, K ^b   Lewis, R J ^a   Murshudov, G N ^a   Verma, C S ^a   Dodson, G G ^a   Wilson, K S ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

^b AB Biotechnologie IITU Hamburg   (Germany)

Author keywords

Autoproteolysis; Mutant precursor; Ntn hydrolase; Penicillin acylase; X ray structure

Indexed keywords

BACTERIAL ENZYME; ENZYME PRECURSOR; PENICILLIN AMIDASE; PENICILLIN G; PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN EXPRESSION; STEREOCHEMISTRY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034730417     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4105     Document Type: Article

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