Histidinol-phosphatase

Histidinol-phosphatase
Histidinol-phosphatase tetramer, Thermus thermophilus
Identifiers
EC no.3.1.3.15
CAS no.9025-79-0
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The enzyme histidinol-phosphatase (EC 3.1.3.15) catalyzes the reaction

2D representation of the chemical structure of Q27102169.
L-histidinol phosphate
 
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27101817.
histidinol

The enzyme characterised from Neurospora crassa hydrolyses L-histidinol phosphate to histidinol and orthophosphate. The reaction is part of the biosynthesis of the amino acid histidine.[1][2][3]

Nomenclature

This enzyme is a hydrolase, specifically one acting on phosphoric monoester bonds. The systematic name is L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase.[4]

E. coli

In E. coli the enzyme encoded by the gene hisB is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.[5]

References

  1. ↑ Ames, Bruce N. (1957). "The biosynthesis of histidine; L-histidinol phosphate phosphatase". Journal of Biological Chemistry. 226 (2): 583–593. doi:10.1016/S0021-9258(18)70840-5. PMID 13438843.
  2. ↑ Ghodge, Swapnil V.; Fedorov, Alexander A.; Fedorov, Elena V.; Hillerich, Brandan; Seidel, Ronald; Almo, Steven C.; Raushel, Frank M. (2013). "Structural and Mechanistic Characterization of l-Histidinol Phosphate Phosphatase from the Polymerase and Histidinol Phosphatase Family of Proteins". Biochemistry. 52 (6): 1101–1112. doi:10.1021/bi301496p. PMC 3570733. PMID 23327428.
  3. ↑ Kinateder, Thomas; Mayer, Carina; Nazet, Julian; Sterner, Reinhard (2024). "Improving enzyme functional annotation by integrating in vitro and in silico approaches: The example of histidinol phosphate phosphatases". Protein Science. 33 (2) e4899. doi:10.1002/pro.4899. PMC 10804674. PMID 38284491.
  4. ↑ Enzyme 3.1.3.15 at KEGG Pathway Database.
  5. ↑ Brilli M, Fani R (February 2004). "Molecular evolution of hisB genes". Journal of Molecular Evolution. 58 (2): 225–237. Bibcode:2004JMolE..58..225B. doi:10.1007/s00239-003-2547-x. PMID 15042344. S2CID 1684458.