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- Title
Dictyostelium phenylalanine hydroxylase is activated by its substrate phenylalanine
- Authors
Kim, Hye-Lim; Park, Mi-Bee; Kim, Yumin; Yang, Yun Gyeong; Lee, Soo-Woong; Zhuang, Ningning; Lee, Kon Ho; Park, Young Shik
- Abstract
Abstract: 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. Structured summary of protein interactions: dicPAH and dicPAH bind by molecular sieving (View Interaction: 1, 2, 3, 4)
- Subjects
DICTYOSTELIUM discoideum; HYDROXYLASES; PHENYLALANINE; ESCHERICHIA coli; TETRAHYDROBIOPTERIN; PHENYLALANINE hydroxylase
- Publication
FEBS Letters, 2012, Vol 586, Issue 20, p3596
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.09.008