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Subcellular localization and properties of kynurenine 3-hydroxylase from eggs ofEphestia kühniella Z.

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Summary

Kynurenine 3-hydroxylase has been studied in isolated mitochondria from ovaries ofEphestia kühniella wild-type and eye color mutants. In the wild-type and three mutants (a, bch andwa) tested, equal activities of kynurenine 3-hydroxylase were found. The enzyme is located in mitochondria and possesses the following characteristics: a requirement for NADPH, but not for NADH; a pH optimum of 8.2;K m values for kynurenine and NADPH are 3.3×10−4M and 1.5×10−4M, respectively; Vmax for kynurenine and NADPH are 5.1 nmol/minxmg and 2.8 nmol/minxmg, respectively. Kinetic analysis of the inhibition indicates that KCN and KCl do not affect enzyme activity at low concentration, but inhibit it at high concentration. Xanthommatin inhibited the kynurenine 3-hydroxylase while kynurenic acid, xanthurenic acid and anthranilic acid had no inhibitory effect.

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  1. Zoologisches Institut der Universität Köln, 1. Lehrstuhl, Weyertal 119, D-5000, Köln 41, Germany

    Emmanuel Stratakis

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Stratakis, E. Subcellular localization and properties of kynurenine 3-hydroxylase from eggs ofEphestia kühniella Z.. J Comp Physiol B 141, 451–456 (1981). https://doi.org/10.1007/BF01101466

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