A new reaction of glutamate dehydrogenase: The enzyme-catalyzed formation of trinitrobenzene from TNBS in the presence of reduced coenzyme

David J. Bates, Barry R. Goldin, Carl Frieden

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Glutamate dehydrogenase is shown to catalyze the reaction of trinitrobenzene sulfonate with DPNH or TPNH to yield trinitrobenzene, sulfite, and DPN or TPN. The reaction is stereospecific with respect to removal of deuterium from the reduced coenzyme and is affected by the same purine nucleotides which affect the normal activity. In addition, the reaction is inhibited by α-ketoglutarate. No chemical modification of amino acid residues occurs during the catalysis. It is concluded that the TNBS reaction occurs at the catalytic site of the enzyme.

Original languageEnglish
Pages (from-to)502-507
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume39
Issue number3
DOIs
StatePublished - May 11 1970

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