Additional Evidence for the Liberation of Substrate α-Hydrogen Prior to Reduction of the Coenzyme in D-Amino Acid Oxidase Reaction
- 1 August 1974
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 76 (2) , 451-454
- https://doi.org/10.1093/oxfordjournals.jbchem.a130587
Abstract
D-Amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3] was reduced by m- and p-methoxyphenylglycine, m- and p-methylphenylglycine, and m-chlorophenylglycine without the appearance of any long-wavelength-absorbing intermediate, as in the case of basic amino acids, though it was reduced by phenylglycine and p-chlorophenylglycine with the appearance of a long-wavelength-absorbing intermediate, as in the case of neutral amino acids. When the logarithms of the rates of reduction of the enzyme with phenylglycine derivatives, in which the enzyme was reduced without appearance of a long-wavelength-absorbing intermediate, were plotted against Hammett's σ-values, a linear correlation with a positive ρ-value was obtained in the range of σ>0. This indicates that the cleavage of the σ-CH bond of the substrate by D-amino acid oxidase occurs via proton transfer prior to the reduction of the coenzyme.MKeywords
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