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1995 (1)
1979 (1)
1Author    Dorothee Petz, H. Ans-G, Erhard Löffler, Friedh SchneiderRequires cookie*
 Title    Inhibition of E. coli l -Asparaginase by Reaction with 2,3-Butanedione. Chemical Modification of Arginine and Histidine Residues  
 Abstract    The inactivation o f E. coli asparaginase by 2,3-butanedione studied with L-asparagine and dia-zooxonorvaline as substrates obeys pseudo first order kinetics. Activity losses are linear with re­ spect to arginine and histidine m odification, with com plete inactivation being correlated with alter­ ation o f one arginine and one histidine per subunit. The rate o f inactivation o f the enzym was re­ duced in the presence o f com petitive inhibitors like L-2-am ino-2-carboxyethane-sulfonam ide. U n ­ der comparable conditions 1,2-cyclo hexanedione does not affect the activity o f L-asparaginase. 
  Reference    Z. Naturforsch. 34c, 742 (1979); received May 8 1979 
  Published    1979 
  Keywords    Asparaginase, 2, 3-Butanedione, Arginine and Histidine Residues 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0742.pdf 
 Identifier    ZNC-1979-34c-0742 
 Volume    34 
2Author    KenjiM. Atsui, H. Iroyuki, S. Hinta, T. Adahiko, K. Ajiwara, A. Kikazu, H. Atan AkRequires cookie*
 Title    Effect of Modification of Arginine Residues on the Activity of Soybean Lipoxygenase-1  
 Abstract    Arginine residues of soybean lipoxygenase-1 was modified with an arginine-directed chemical modifier, 2,3-butanedione. Although inactivation was not visible if the enzyme reac­ tion was monitored under the standard assay condition (83.3 |.im linoleic acid dispersed in 200 mM sodium borate, pH 9.0), rapid inactivation was observed with 5 mM sodium borate, pH 8.0. The inactivation was protected by the addition of a substrate, linoleic acid, in the modification mixture. Kinetic analyses indicated that one arginine residue accounted for the inactivation. Enzymological analyses showed that the modification narrowed the pH-activity profile of L-l and made L-l sensitive to salt concentration of the assay solution. Strong inactivation by modification was found at low salt concentration and low pH. This was not due to a physical change of the linoleic acid. On the other hand, product specificity of L-l was not altered after modification. Taken together, the modified arginine residue(s) was thought to be not essential to the catalysis but have an important role in supporting an ideal electrostatic interaction within L-l and/or between L-l and a substrate even in sub-optimal reaction conditions. 
  Reference    Z. Naturforsch. 50c, 37—4 (1995); received September 26/November 8 1994 
  Published    1995 
  Keywords    Arginine, 2, 3-Butanedione, Modification, Soybean Lipoxygenase-1 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0037.pdf 
 Identifier    ZNC-1995-50c-0037 
 Volume    50