Go toArchive
Browse byFacets
Bookbag ( 0 )
'Dehydrogenases' in keywords
Results  2 Items
Sorted by   
Section
Publication Year
1981 (1)
1974 (1)
1Author    Reinhard Jeck, Christoph WoenckhausRequires cookie*
 Title      
 Abstract    The coenzyme anologues [3-(2-acetylpyridinio) -propyl]-adenosine pyrophosphate and [3-(2-bromo-acetylpyridinio) -propyl] -adenosine pyrophoshate were synthesized and used for inhibition studies. While the first compound reacts as competitive inhi­ bitor against NAD+ , the latter is able to form co­ valently bound derivatives of several NAD+ -depen-dent dehydrogenases, giving informations about amino acid side chains participating in the binding of the functional coenzyme part. [3-(2-acetylpyridinio) -propyl] -adenosine pyro­ phosphate exhibits strong hypochromicity between adenine and 2-acetylpyridine ring. Cleavage of the pyrophosphate bridge increases the absorption at 261 nm up to 22% and indicates, that the stacked configuration of the molecule is preferred in aqueous solution. In enzymatic assays with YADH and GAPDH [3-(2-acetylpyridinio) -propyl] -adenosine pyrophos­ phate acts as a competitive inhibitor against NAD+ . The inhibition constants are: Xi = 1.7'10-2 M (YADH) and 4.3, 10" 4m (GAPDH) and show, that the coenzyme analogue has little affinity to the co­ enzyme binding sites. Difference spectra of the coenzyme-enzyme mixtures and the isolated com­ ponents do not show any spectral changes due to the formation of the binary complex in the case of YADH and only small effects with GAPDH. From this results it can be concluded, that the incorpora­ tion of the 2-acetylpyridinio-propyl residue into the enzymes is sterically hindered. This is also indicated by the fact, that YADH shows smaller inhibition constants with adenosine monophosphate and adeno­ sine diphosphate 1. We obtained [3-(2-bromoacetylpyridinio) -pro­ pyl]-adenosine pyrophosphate by bromination of 
  Reference    (Z. Naturforsch. 29c, 180 [1974]; received) 
  Published    1974 
  Keywords    ) N AD+ -analogues, Dehydrogenases, Inhibition, Affinity Labelling 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/29/ZNC-1974-29c-0180_n.pdf 
 Identifier    ZNC-1974-29c-0180_n 
 Volume    29 
2Author    Rainer Jaenicke, Hans-Dietrich Liidemann, Gerhard SchmidRequires cookie*
 Title    Pressure, Temperature and pH Dependence of the Absorption Spectrum of Reduced Nicotinamide Adenine Dinucleotide  
 Abstract    Enzymological studies at high hydrostatic pressure generally involve temperature, pH and pressure as variables, owing to the effect of adiabatic compression and the ionization volume o f the buffer system. In the case of N AD dependent oxidoreductases this implies that the extinction coefficient o f the coenzyme may be affected by p, T and pH, apart from the spectral change accompanying the redox reaction. Measurements o f the pressure dependence of the absorbance of N AD H show a slight red shift and a 1% decrease (3% increase) o f the absorbance at 339 nm (360 nm) at 2 kbar. The pH depen­ dence at the given wavelengths amounts to —(2.4 ± 0.1)% per pH unit (25 °C), while the intrinsic temperature effect (after correction for thermal expansion) is o f the order o f -0.2% per degree (2 0 -3 0 °C). Applying buffers with negligible ionization volume, 366 nm is the optimum wavelength for high pressure studies up to 2 kbar because here the pressure dependent spectral changes o f the N ADH absorption vanish. 
  Reference    Z. Naturforsch. 36c, 84—8 (1981); received October 9 1980 
  Published    1981 
  Keywords    Absorption, Dehydrogenases, High Pressure, NADH, Oxidoreductases, pH Dependence, Tem­ perature Dependence 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0084.pdf 
 Identifier    ZNC-1981-36c-0084 
 Volume    36