Substrates with charged residues are efficiently hydrolyzed by serine carboxypeptidases when S3-P1 interactions are facilitated

Biochemistry

Volumn 36, Issue 40, 1997, Pages 12235-12241

  Olesen, Kjeld ^a   Breddam, Klaus ^a  

^a CARLSBERG LABORATORY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; MUTANT PROTEIN; SERINE CARBOXYPEPTIDASE; CARBOXYPEPTIDASE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PH; PRIORITY JOURNAL; BINDING SITE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; OSMOLARITY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

BINDING SITES; CARBOXYPEPTIDASES; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MUTAGENESIS, SITE-DIRECTED; OSMOLAR CONCENTRATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 0030610045     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971020p     Document Type: Article

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