The action of alpha-ketoglutarate dehydrogenase on 4-chloronitrosobenzene: evidence for species-dependent differences in active site properties.
The reaction of bovine (Bos taurus) and porcine (Sus scrufa) cardiac alpha-ketoglutarate dehydrogenase complex (alpha-KGD) with 4-chloronitrosobenzene (I) was shown to produce a hydroxamic acid (IV) and a product due to a Bamberger rearrangement as previously shown for Escherichia coli alpha-KGD. The conversion of I into an active site-bound electrophile was general among the three alpha-KGD enzymes tested, but quantitative differences in products and kinetics were shown. The reaction of I was specific for the resolved alpha-ketoglutarate decarboxylase subunit.
Doerge
D R
DR
Corbett
M D
MD
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology; D066298:In Vitro Techniques; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D009603:Nitroso Compounds / Q000378:metabolism*; D013045:Species Specificity; D013552:Swine
D009603:Nitroso Compounds; C018484:4-chloronitrosobenzene; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex