• BMB Reports
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• v.41 no.5
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• pp.408-413
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• 2008

Pyridoxal-5'-phosphate phosphatase (PLPP) catalyzes the dephosphorylation of pyridoxal-5'-phosphate (PLP). A human brain PLPP gene was fused with a PEP-1 peptide and produced a genetic in-frame PEP-1-PLPP fusion protein. The purified PEP-1-PLPP fusion protein was efficiently transduced into PC12 cells in a time- and dose-dependent manner when added exogenously to culture media. Once inside the cells, the transduced PEP-1-PLPP fusion protein was stable for 36 h. The concentration of PLP was markedly decreased by the addition of exogenous PEP-1-PLPP to media pretreated with the vitamin $B_6$ precursors; pyridoxine, pyridoxal kinase and pyridoxine-5'-phosphate oxidase into cells. The results suggest that the transduction of the PEP-1-PLPP fusion protein can be one mode of PLP level regulation, and to replenish this enzyme in the various neurological disorders related to vitamin $B_6$.

• Journal of the Korean Ceramic Society
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• v.36 no.2
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• pp.186-192
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• 1999

Dang-Chin feldspar powder with the mean particle size of 9.1 $\mu\textrm{m}$ was added to the synthesized mullite powder with the particle size of +325∼-200 mesh and the powder compact was prepared by PLPP(pressureless powder packing method). Densification behaviors were observed in sintering temperature range of 1200∼1400$^{\circ}C$. The binder solution of 4% PVA was infilterated into packed powder to the suitable strength. The PLPP method makes it possible to form compacts without clay as plasticizer. Therfore there was no defect caused by phase transition after sintering. Additionally, we observed the dense microstructure by the melting of feldspar. When the mullite compacts with feldspar of 30% were sintered at 1300$^{\circ}C$-4 hrs, we obtained the dense microstructure with zero water absorption and porosity <1%. When these compacts were sintered longer than 4 hrs at 1300$^{\circ}C$ or higher than 1400$^{\circ}C$, the examggerated grain growth of mullite was observed.

• Journal of Life Science
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• v.18 no.4
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• pp.585-589
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• 2008

Chronophin is a phosphatase responsible for the dephosphorylation of cofilin, which regulates the rearrangement of actin cytoskeleton. It is also known as a phosphatase for pyrodoxal 5'-phosphate (PLP), an active form of vitamin $B_6$, and maintains the level of PLP in the cytoplasm. Since this phosphatase belongs to a HAD subfamily containing a cap domain, it is expected to undergo a conformational change for the binding of a substrate. However, the crystal structure of chronophin has a disulfide bridge between the cap and core domains preventing a movement of the cap domain against the core domain. It is possible that the disulfide bond between C91 and C221 was formed by an oxidation during the crystallization. Here, we obtained chronophin crystals under a reduced condition and determined the crystal structure. This reduced chronophin does not contain a disulfide bridge and shows a closed conformation like the oxidized form. It implies that an active chronophin binds its substrate under the closed conformation without the disulfide bond and shows a high substrate specificity in the cell.