Abstract
IN our series of investigations on the formation of an apo-enzyme–coenzyme–substrate complex of D-amino-acid oxidase1–3, we set out to examine the Michaelis complex of this enzyme to elucidate the mechanism of enzyme action. For this purpose we have been striving to isolate a model of the Michaelis complex. Normally, real substrate is oxidized by the enzyme, so we used a ‘substrate-substitute’, which combines with the enzyme in the same way as real substrate but is not attacked by the enzyme.
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References
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YAGI, K., OZAWA, T. Formation of D-Amino-acid Oxidase Artificial Michaelis Complex. Nature 193, 483–484 (1962). https://doi.org/10.1038/193483a0
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DOI: https://doi.org/10.1038/193483a0
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