Pyridoxal /Pyridoxine Vitamin B6 -Phosphatase (PDXP) ELISA Kit for Mouse

Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. The preferred degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP (Jang et al., 2003 [PubMed 14522954]).[supplied by OMIM, Mar 2008]

PDXP: Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. Homodimer. Ubiquitous. Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain. Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. Belongs to the HAD-like hydrolase superfamily.

Protein type: Cofactor and Vitamin Metabolism - vitamin B6; Cell cycle regulation; EC 3.1.3.3; EC 3.1.3.74; Protein phosphatase, Ser/Thr (non-receptor)

Chromosomal Location of Human Ortholog: 22q12.3

Cellular Component: lamellipodium; plasma membrane; midbody; cytosol; cleavage furrow; actin cytoskeleton

Molecular Function: protein binding; phosphoserine phosphatase activity; heat shock protein binding; magnesium ion binding; phosphoprotein phosphatase activity; pyridoxal phosphatase activity

Biological Process: actin rod formation; positive regulation of actin filament depolymerization; regulation of mitosis; pyridoxal phosphate catabolic process; protein amino acid dephosphorylation; regulation of cytokinesis