Neutralization of acidic residues in helix II stabilizes the folded conformation of acyl carrier protein and variably alters its function with different enzymes

Journal of Biological Chemistry

Volumn 282, Issue 7, 2007, Pages 4494-4503

  Gong, Huansheng ^a   Murphy, Anne ^a   McMaster, Christopher R ^a   Byers, David M ^a,b  

^a DALHOUSIE UNIVERSITY   (Canada)

^b DALHOUSIE UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; CONFORMATIONS; ENZYME KINETICS; FATTY ACIDS; PATHOGENS;

ACYL CARRIER PROTEIN (ACP); BACTERIAL GROWTH; DIVALENT CATIONS; PATHOGENESIS;

PROTEIN FOLDING;

ACYL ACP SYNTHETASE; ACYL CARRIER PROTEIN; AMIDE; AMINO ACID; ASPARAGINE; DIVALENT CATION; FATTY ACID; GLUTAMINE; HOLOACYL ACP SYNTHASE; MAGNESIUM ION; MUTANT PROTEIN; PROTEIN DERIVATIVE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE ACYLTRANSFERASE; ACYL (ACYL CARRIER PROTEIN) UDP N ACETYLGLUCOSAMINE ACYLTRANSFERASE; ACYL-(ACYL-CARRIER-PROTEIN)-UDP-N-ACETYLGLUCOSAMINE ACYLTRANSFERASE; ACYLTRANSFERASE; BACTERIAL PROTEIN; HOLO (ACYL CARRIER PROTEIN) SYNTHASE; HOLO-(ACYL-CARRIER-PROTEIN) SYNTHASE; MAGNESIUM; PHOSPHOTRANSFERASE;

ACIDITY; ACYLATION; ARTICLE; BINDING SITE; ENZYME ACTIVITY; GENE MUTATION; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; VIBRIO HARVEYI; CHEMISTRY; GENETICS; METABOLISM; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; VIBRIO;

BACTERIA (MICROORGANISMS); VIBRIO HARVEYI;

ACYL CARRIER PROTEIN; ACYLTRANSFERASES; BACTERIAL PROTEINS; BINDING SITES; CATIONS, DIVALENT; HYDROGEN-ION CONCENTRATION; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFERASES (OTHER SUBSTITUTED PHOSPHATE GROUPS); VIBRIO;

EID: 33947504254     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M608234200     Document Type: Article

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