Dictyostelium phenylalanine hydroxylase is activated by its substrate phenylalanine.

We have studied the regulatory function of Dictyostelium discoideum Ax2 phenylalanine hydroxylase (dicPAH) via characterization of domain structures. Including the full-length protein, partial proteins truncated in regulatory, tetramerization, or both, were prepared from Escherichia coli as his-tag proteins and examined for oligomeric status and catalytic parameters for phenylalanine. The proteins were also expressed extrachromosomally in the dicPAH knockout strain to examine their in vivo compatibility. The results suggest that phenylalanine activates dicPAH, which is functional in vivo as a tetramer, although cooperativity was not observed. In addition, the results of kinetic study suggest that the regulatory domain of dicPAH may play a role different from that of the domain in mammalian PAH. Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Hye-Lim Kim, Mi-Bee Park, Yumin Kim, Yun Gyeong Yang, Soo-Woong Lee, Ningning Zhuang, Kon Ho Lee, Young Shik Park. Dictyostelium phenylalanine hydroxylase is activated by its substrate phenylalanine. FEBS letters. 2012 Oct 19;586(20):3596-600

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PMID: 23017206

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