Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family

Journal of Molecular Biology

Volumn 397, Issue 1, 2010, Pages 249-259

  Kerff, Frédéric ^a   Petrella, Stéphanie ^a   Mercier, Frédéric ^a   Sauvage, Eric ^a   Herman, Raphaël ^a   Pennartz, Anne ^a   Zervosen, Astrid ^a   Luxen, André ^a   Frère, Jean Marie ^a   Joris, Bernard ^a   Charlier, Paulette ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

amidase activity; lipoprotein; metallo enzyme; peptidoglycan metabolism; peptidoglycan recognition protein (PGRP)

Indexed keywords

AMIDASE; APOENZYME; HOLOENZYME; LYSOZYME; N ACETYLMURAMOYLALANINE AMIDASE; N ACETYLMURAMOYLALANINE AMIDASE AMID; PEPTIDOGLYCAN; UNCLASSIFIED DRUG; ZINC AMIDASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE T7; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENE INSERTION; HYDROLYSIS; LIPID ANALYSIS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY;

AMIA; ESCHERICHIA COLI;

EID: 77249102992     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.12.038     Document Type: Article

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