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Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants.

par Prévost, Martine ;Chvalun, Sergei;Tulkens, Paul M.;Courvalin, P;Van Bambeke, Françoise
Référence Journal of molecular microbiology and biotechnology, 2, 3, page (321-330)
Publication Publié, 2000-07

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Titre:	Modeling of Enterococcus faecalis D-alanine:D-alanine ligase: structure-based study of the active site in the wild-type enzyme and in glycopeptide-dependent mutants.
Auteur:	Prévost, Martine; Chvalun, Sergei; Tulkens, Paul M.; Courvalin, P; Van Bambeke, Françoise
Informations sur la publication:	Journal of molecular microbiology and biotechnology, 2, 3, page (321-330)
Statut de publication:	Publié, 2000-07
Sujet CREF:	Chimie
MeSH keywords:	Adenosine Diphosphate -- metabolism
	Amino Acid Sequence
	Binding Sites
	Catalytic Domain
	Enterococcus faecalis -- enzymology
	Enterococcus faecalis -- genetics
	Escherichia coli -- enzymology
	Glycopeptides -- metabolism
	Magnesium -- metabolism
	Models, Molecular
	Molecular Sequence Data
	Mutation
	Peptide Synthases -- chemistry
	Peptide Synthases -- genetics
	Peptide Synthases -- metabolism
	Phosphates -- chemistry
	Phosphates -- metabolism
	Phosphines -- chemistry
	Phosphines -- metabolism
	Protein Conformation
	Sequence Homology, Amino Acid
	Structure-Activity Relationship
Note générale:	Journal Article
	Research Support, Non-U.S. Gov't
	SCOPUS: ar.j
Langue:	Anglais
Identificateurs:	urn:issn:1464-1801
	info:scp/0342264622
	info:pmid/10937441