OMP decarboxylase: An experimental test of electrostatic destabilization of the enzyme-substrate complex

Journal of the American Chemical Society

Volumn 126, Issue 45, 2004, Pages 14698-14699

  Callahan, Brian P ^a   Wolfenden, Richard ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CARBOXYLIC ACID; CARBOXYLYASE;

ADSORPTION; AMINO ACID SEQUENCE; ANION EXCHANGE CHROMATOGRAPHY; AQUEOUS SOLUTION; ARTICLE; BINDING AFFINITY; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYST; CHEMICAL REACTION; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; ELECTRIC POTENTIAL; ENERGY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGENATION; LIGAND BINDING; MOLECULAR INTERACTION; MOLECULAR STABILITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PKA; REACTION ANALYSIS; TECHNIQUE;

ELECTROSTATICS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; LIGANDS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OROTIDINE-5'-PHOSPHATE DECARBOXYLASE; URIDINE MONOPHOSPHATE;

EID: 8844240654     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0450049     Document Type: Article

References (18)

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7. + refers to the form of the inhibitor where the amino group is positively charged, and MAUMP refers to the form where the amino group is neutral.
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