Specificity and Reactivity in Menaquinone Biosynthesis: The Structure of Escherichia coli MenD (2-Succinyl-5-Enolpyruvyl-6-Hydroxy-3-Cyclohexadiene-1-Carboxylate Synthase)

Journal of Molecular Biology

Volumn 384, Issue 5, 2008, Pages 1353-1368

  Dawson, Alice ^a   Fyfe, Paul K ^a   Hunter, William N ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

crystal structure; enzyme mechanism; menaquinone biosynthesis; thiamine diphosphate cofactor

Indexed keywords

2 OXOGLUTARIC ACID; AMINO ACID; BACTERIAL ENZYME; COCARBOXYLASE; MANGANESE; MENAQUINONE; MEND ENZYME; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVATION; ENZYME BINDING; ENZYME DEGRADATION; ENZYME REACTIVATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; VITAMIN METABOLISM;

ESCHERICHIA COLI; MAMMALIA;

EID: 56949084464     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.048     Document Type: Article

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