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J. Biol. Chem., Vol. 278, Issue 50, 50040-50046, December 12, 2003

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Human Pyridoxal Phosphatase

MOLECULAR CLONING, FUNCTIONAL EXPRESSION, AND TISSUE DISTRIBUTION^*

Young Min Jang, Dae Won Kim, Tae-Cheon Kang¶, Moo Ho Won¶, Nam-In Baek||, Byung Jo Moon, Soo Young Choi**, and Oh-Shin Kwon

From the Department of Biochemistry, Kyungpook National University, Taegu 702-701, Korea, the Department of Genetic Engineering, Division of Life Sciences, Hallym University, Chunchon 200-702, Korea, the ^¶Department of Anatomy, College of Medicine, Hallym University, Chunchon 200-702, Korea, and the ^||Graduate School of Biotechnology & Plant Metabolism Research Center, Kyunghee University, Suwon 449-701, Korea

Pyridoxal phosphatase catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP) and pyridoxine 5'-phosphate. A human brain cDNA clone was identified to the PLP phosphatase on the basis of peptide sequences obtained previously. The cDNA predicts a 296-amino acid protein with a calculated M_r of 31698. The open reading frame is encoded by two exons located on human chromosome 22q12.3, and the exon-intron junction contains the GT/AG consensus splice site. In addition, a full-length mouse PLP phosphatase cDNA of 1978 bp was also isolated. Mouse enzyme encodes a protein of 292 amino acids with M_r of 31512, and it is localized on chromosome 15.E1. Human and mouse PLP phosphatase share 93% identity in protein sequence. A BLAST search revealed the existence of putative proteins in organism ranging from bacteria to mammals. Catalytically active human PLP phosphatase was expressed in Escherichia coli, and characteristics of the recombinant enzyme were similar to those of erythrocyte enzyme. The recombinant enzyme displayed K_m and k_cat values for pyridoxal of 2.5 µM and 1.52 s^–1, respectively. Human PLP phosphatase mRNA is differentially expressed in a tissue-specific manner. A single mRNA transcript of 2.1 kb was detected in all human tissues examined and was highly abundant in the brain. Obtaining the molecular properties for the human PLP phosphatase may provide new direction for investigating metabolic pathway involving vitamin B₆.

Received for publication, August 29, 2003 , and in revised form, September 22, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY125047 and AY366300.

^* This work was supported by Grant R01-2002-000-00008-0 from the Basic Research Program of the Korea Science & Engineering Foundation and Korea Health 21 R&D Project Grant (02-PJ1-PG10-20706-0002) from the Ministry of Health and Welfare, Korea. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence may be addressed. E-mail: sychoi{at}hallym.ac.kr. To whom correspondence may be addressed: Dept. of Biochemistry, Kyungpook National University, Taegu, 702-701, Korea. Tel.: 82-53-950-6356; Fax: 82-53-943-2762; E-mail: oskwon{at}knu.ac.kr.

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