A cDNA encoding Pyridoxine 5'-phosphate oxidase (PNPO) from Bombyx mori was cloned and characterized (GenBank accession number: DQ452398). The cDNA encodes a polypeptide of 257 amino acid residues. The recombinant enzyme purified from Escherichia coli exhibited maximal activity at pH 9.0, and the K(m) values for the substrates of pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate were determined as 0.65 and 1.15 micromol/l. It was found that B. mori PNPO shares 51.44% homology with humans, but several function-related, key amino acid residues in B. mori PNPO are different from the human and E. Coli gene. B. mori has a single copy of the PNPO gene, which spans a 3.5 kb region and contains five exons and four introns. B. mori PNPO is a homodimer, with each monomer containing nine antiparallel beta-strands and five alpha-helical segments. The secondary structure was deduced from computational study.
Copper is an essential micronutrient as its redox properties play a significant biochemistry role in the nervous system. Its essentiality is evidenced by Menkes disease (MD), an X-linked neurodegenerative disease caused by mutations in the ATP7A copper transporter, showing that ATP7A is concerned with the development of the nervous system. To investigate the regulation of ATP7A in the development of neurons, we analyzed the expression of the mRNA, protein and the localization of ATP7A in C57BL/6 mice neural stem cells (NSCs), astrocytes and hippocampal neurons cultured in vitro. The results indicated that ATP7A expression was decreased stepwise in NSC, astrocytes and hippocampal neurons. The fluorescent signals of ATP7A were located between the nucleus and plasma membrane in the three kinds of cells. It can be concluded that ATP7A might be involved in the development of neurons and astrocytes. This research may contribute to knowledge about the severe neurodegeneration characteristic of copper-metabolic diseases caused by mutations in the ATP7A gene.
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