TY - JOUR
T1 - A new reaction of glutamate dehydrogenase
T2 - The enzyme-catalyzed formation of trinitrobenzene from TNBS in the presence of reduced coenzyme
AU - Bates, David J.
AU - Goldin, Barry R.
AU - Frieden, Carl
N1 - Funding Information:
The research supported by Grant No. ~8-1568 R from the National Science Foundation. The mass spectrometer was supported from HSAA grant 4 FR 06115, National Institutes of Health. NDEA Predoctoral Fellow U.S. Public Health Service Postdoctoral Fellow GM39,280
PY - 1970/5/11
Y1 - 1970/5/11
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0014941295&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(70)90606-6
DO - 10.1016/0006-291X(70)90606-6
M3 - Article
C2 - 4393049
AN - SCOPUS:0014941295
SN - 0006-291X
VL - 39
SP - 502
EP - 507
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -