Letter | Published:

Formation of D-Amino-acid Oxidase Artificial Michaelis Complex

Naturevolume 193pages483484 (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.

References

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    Yagi, K., Ozawa, T., and Harada, M., Nature, 184, 1938 (1959).

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    Yagi, K., and Ozawa, T., Biochim. Biophys. Acta, 42, 381 (1960).

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    Yagi, K., and Ozawa, T., Biochim. Biophys. Acta (in the press).

  4. 4

    Yagi, K., Ozawa, T., and Harada, M., Nature, 188, 745 (1960).

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    Yagi, K., and Ozawa, T., Nature, 192, 70 (1961).

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    Yagi, K., and Ozawa, T., Biochim. Biophys. Acta (in the press).

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Affiliations

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

    • KUNIO YAGI
    •  & TAKAYUKI OZAWA

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

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