Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site

Structure

Volumn 4, Issue 3, 1996, Pages 253-264

  Leesong, Minsun ^a   Henderson, Barry S ^b,c   Gillig, James R ^b,d   Schwab, John M ^b,e   Smith, Janet L ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d ELI LILLY AND COMPANY   (United States)

^e CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

Author keywords

Bifunctional enzyme; Crystal structure; Dehydratase; Fatty acid biosynthesis; Isomerase; Suicide inhibition

Indexed keywords

3 DECYNOYL N ACETYLCYSTEAMINE; 3-DECYNOYL-N-ACETYLCYSTEAMINE; DRUG DERIVATIVE; MERCAPTAMINE; PREPHENATE DEHYDRATASE; RECOMBINANT PROTEIN;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; METABOLISM; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

BINDING SITES; CRYSTALLIZATION; CYSTEAMINE; ESCHERICHIA COLI; MODELS, MOLECULAR; PREPHENATE DEHYDRATASE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030584655     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00030-5     Document Type: Article

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