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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The active site of L-asparaginase: dimethylsulfoxide effect of 5-diazo-4-oxo-L-norvaline interactions.

The asparagine analog, 5-diazo-4-oxo-L-norvaline is a substrate and an irreversible inhibitor of L-asparaginase. Covalent attachment occurs at an increased rate at concentrations of dimethylsulfoxide which reduce the catalytic decomposition of diazo-oxo-norvaline. In 55% dimethylsulfoxide asparaginase is inactivated by diazo-oxo-norvaline (0.05 M) with a t 1/2 of twelve seconds. In aqueous buffer the rate of diazo-oxo-norvaline decomposition is increased three-fold in the presence of the nucleophile hydroxylamine; this nucleophile also protects the enzyme against inactivation by diazo-oxo-norvaline in the presence of dimethylsulfoxide.[1]

References

  1. The active site of L-asparaginase: dimethylsulfoxide effect of 5-diazo-4-oxo-L-norvaline interactions. Lachman, L.B., Handschumacher, R.E. Biochem. Biophys. Res. Commun. (1976) [Pubmed]
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