Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis

Biochemistry

Volumn 47, Issue 19, 2008, Pages 5290-5302

  Bartling, Craig M ^a   Raetz, Christian R H ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYST ACTIVITY; ESCHERICHIA COLI; POSITIVE IONS; PROTEINS;

HOMOGENEITY; NONCOMPETITIVE INHIBITORS; STEADY STATE KINETICS; URACIL MOIETY;

LIPIDS;

ACYLTRANSFERASE; BASE; DIVALENT CATION; GLUCOSAMINE DERIVATIVE; LIPID A; LPXD PROTEIN; PANTETHEINE; URACIL;

ACYLATION; ARTICLE; BINDING AFFINITY; BIOSYNTHESIS; CATALYSIS; CHLAMYDIA TRACHOMATIS; ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR RECOGNITION; MUTAGENESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STEADY STATE; X RAY;

ACYL CARRIER PROTEIN; ACYLTRANSFERASES; BACTERIAL PROTEINS; CATALYSIS; CHLAMYDIA TRACHOMATIS; ENZYME INHIBITORS; ESCHERICHIA COLI; KINETICS; LIGANDS; LIPID A; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN;

CHLAMYDIA TRACHOMATIS; ESCHERICHIA COLI;

EID: 43249099873     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800240r     Document Type: Article

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