Molecular recognition by Escherichia coli UDP-3-O-(R-3-hydroxymyristoyl)-N- acetylglucosamine deacetylase is modulated by bound metal ions

Biochemistry

Volumn 45, Issue 49, 2006, Pages 14573-14581

  Hernick, Marcy ^a   Fierke, Carol A ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BIOSYNTHESIS; ENZYME IMMOBILIZATION; ESCHERICHIA COLI; FATTY ACIDS; LIPIDS;

ACETATES; LIGANDS; METAL IONS; MOLECULAR RECOGNITION;

MOLECULAR BIOLOGY;

ACETIC ACID; ACYL GROUP; ANTIBIOTIC AGENT; ENZYME; ENZYME INHIBITOR; FATTY ACID; FUNCTIONAL GROUP; GLUCOSAMINE DERIVATIVE; HYDROXYMYRISTOYL GROUP; LIGAND; LIPID A; METAL; METAL ION; MYRISTIC ACID; PALMITIC ACID; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE INHIBITOR; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL)GLUCOSAMINE; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL)N ACETYLGLUCOSAMINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CATALYSIS; DRUG DESIGN; DRUG EFFICACY; DRUG SCREENING; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ESCHERICHIA COLI; FLUORESCENCE; GRAM NEGATIVE INFECTION; IN VITRO STUDY; IN VIVO STUDY; LIPOGENESIS; METAL BINDING; MOLECULAR MIMICRY; MOLECULAR RECOGNITION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; SEQUENCE HOMOLOGY;

AMIDOHYDROLASES; BINDING SITES; CATIONS, DIVALENT; ESCHERICHIA COLI; FATTY ACIDS, NONESTERIFIED; KINETICS; METALS; MODELS, MOLECULAR; PALMITIC ACID; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 33845398833     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061625y     Document Type: Article

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