Histidinol-phosphatase

In enzymology, a histidinol-phosphatase (EC 3.1.3.15) is an enzyme that catalyzes the chemical reaction

L-histidinol phosphate + H₂O L-histidinol + phosphate

Thus, the two substrates of this enzyme are L-histidinol phosphate and H₂O, whereas its two products are L-histidinol and phosphate.

This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name of this enzyme class is L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase. This enzyme participates in histidine metabolism.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2FPR, 2FPS, 2FPU, 2FPW, and 2FPX.

E. coli

In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.^[1]

References

• AMES BN (1957). "The biosynthesis of histidine; L-histidinol phosphate phosphatase". J. Biol. Chem. 226 (2): 583–93. PMID 13438843.