Letter | Published:

Formation of D-Amino-acid Oxidase Artificial Michaelis Complex

Nature volume 193, pages 483484 (03 February 1962) | Download Citation

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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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Author information

Affiliations

  1. Department of Biochemistry, School of Medicine, Nagoya University, Nagoya.

    • KUNIO YAGI
    •  & TAKAYUKI OZAWA

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DOI

https://doi.org/10.1038/193483a0

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