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Dictyostelium phenylalanine hydroxylase is activated by its substrate phenylalanine |
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| Authors: | Hye-Lim KimMi-Bee Park Yumin KimYun Gyeong Yang Soo-Woong LeeNingning Zhuang Kon Ho Lee Young Shik Park |
| Affiliation: | a FIRST Research Group, School of Biological Sciences, Inje University, Kimhae 621-749, Republic of Korea b Advanced Research Center for Multiple Myeloma, College of Medicine, Inje University, Busan 614-735, Republic of Korea c Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju 660-701, Republic of Korea d PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea e Department of Microbiology, School of Medicine, Gyeongsang National University, Jinju 660-751, Republic of Korea |
| 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 interactionsdicPAH and dicPAHbind by molecular sieving (View Interaction: 1, 2, 3, 4) |
| Keywords: | BH4, l-erythro-tetrahydrobiopterin DH4, tetrahydrodictyopterin (d-threo-tetrahydrobiopterin) PAH, phenylalanine hydroxylase Phe, l-phenylalanine Tyr, l-tyrosine |
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