Chorismate mutase/prephenate dehydrogenase: protection of the active site(s) against inactivation by iodoacetamide [proceedings]. 1979

E Heyde

UI MeSH Term Description Entries
D007460 Iodoacetamide An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.
D007461 Iodoacetates Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research. Iodoacetic Acids,Acids, Iodoacetic
D007700 Kinetics The rate dynamics in chemical or physical systems.
D011302 Prephenate Dehydratase An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of phenylalanine. EC 4.2.1.51. Chorismate Mutase-Prephenate Dehydratase,Prephenate Hydro-lyase,Chorismate Mutase Prephenate Dehydratase,Dehydratase, Chorismate Mutase-Prephenate,Dehydratase, Prephenate,Hydro-lyase, Prephenate,Mutase-Prephenate Dehydratase, Chorismate,Prephenate Hydro lyase
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D004754 Enterobacter Gram-negative gas-producing rods found in feces of humans and other animals, sewage, soil, water, and dairy products.
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006836 Hydro-Lyases Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1. Dehydratase,Dehydratases,Hydrase,Hydrases,Hydro Lyase,Hydro-Lyase,Hydro Lyases,Lyase, Hydro,Lyases, Hydro
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

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E Heyde
January 1987, Methods in enzymology,
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