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Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors

par Wouters, Johan ;Oudjama, Yamina;Barkley, Sam J.;Tricot, Catherine ;Stalon, Victor ;Droogmans, Louis ;Poulter, C. Dale
Référence The Journal of biological chemistry, 278, 14, page (11903-11908)
Publication Publié, 2003-04

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Titre:	Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors
Auteur:	Wouters, Johan; Oudjama, Yamina; Barkley, Sam J.; Tricot, Catherine; Stalon, Victor; Droogmans, Louis; Poulter, C. Dale
Informations sur la publication:	The Journal of biological chemistry, 278, 14, page (11903-11908)
Statut de publication:	Publié, 2003-04
Sujet CREF:	Sciences bio-médicales et agricoles
MeSH keywords:	Carbon-Carbon Double Bond Isomerases -- antagonists & inhibitors
	Carbon-Carbon Double Bond Isomerases -- chemistry
	Carbon-Carbon Double Bond Isomerases -- metabolism
	Catalytic Domain
	Crystallography
	Cysteine -- chemistry
	Epoxy Compounds -- pharmacology
	Escherichia coli -- enzymology
	Glutamic Acid -- chemistry
	Kinetics
	Organophosphorus Compounds -- pharmacology
	Protein Structure, Secondary
	Tyrosine -- chemistry
Note générale:	Journal Article
	Research Support, Non-U.S. Gov't
	Research Support, U.S. Gov't, P.H.S.
	SCOPUS: ar.j
Langue:	Anglais
Identificateurs:	urn:issn:0021-9258
	info:doi/10.1074/jbc.M212823200
	info:pii/M212823200
	info:scp/0038485617
	info:pmid/12540835
	VX-005389