Investigating the geminal diamine intermediate of Yersinia pestis arginine decarboxylase with substrate, product, and inhibitors using single wavelength stopped-flow spectroscopy

Biochemistry

Volumn 46, Issue 2, 2007, Pages 379-386

  Counts, Korie G ^a   Wong, Isaac ^b   Oliveira, Marcos A ^a  

^a University of Kentucky   (United States)

^b UNIVERSITY OF KENTUCKY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL STATES; GEMINAL DIAMINE INTERMEDIATE; SINGLE WAVELENGTH STOPPED FLOW SPECTROSCOPY; YERSINIA PESTIS ARGININE DECARBOXYLASE;

AMINO ACIDS; ENZYME INHIBITION; MOLECULAR STRUCTURE; PH EFFECTS; REACTION KINETICS; SPECTROSCOPIC ANALYSIS;

ENZYME KINETICS;

AGMATINE; ALDIMINE; ARGININE DECARBOXYLASE; ENZYME; ENZYME INHIBITOR; LIGAND; MAGNESIUM; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; LIGAND BINDING; METHODOLOGY; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS; SINGLE WAVELENGTH STOPPED FLOW SPECTROSCOPY; SPECTROSCOPY; YERSINIA PESTIS;

AGMATINE; ARGININE; CARBOXY-LYASES; CATALYTIC DOMAIN; DIAMINES; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; YERSINIA PESTIS;

YERSINIA PESTIS;

EID: 33846233877     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061260h     Document Type: Article

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