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Literature summary extracted from

  • Ruszkowski, M.; Dauter, Z.
    Structural studies of Medicago truncatula histidinol phosphate phosphatase from inositol monophosphatase superfamily reveal details of penultimate step of histidine biosynthesis in plants (2016), J. Biol. Chem., 291, 9960-9973 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.15 purified enzyme in complex with products histidiol or phosphate, or substrate histidinol phosphate with Mg2+, or Lys-CH2-Cys, sitting drop vapor diffusion, mixing of 19 mg/ml protein solution with crystallization solution containing 15% PEG 3350, and 0.2 M diammonium hydrogen phosphate, pH 8.0, or 30% PEG 3350, 0.1 M Bis-Tris, pH 6.5, 0.2 M ammonium acetate, and 10 mM magnesium acetate, over the reservoir supplemented with 100 mM formaldehyde to complete cross-linking between Lys158 and Cys245 and vitrified in Paraton-N, X-ray diffraction structure determination and analysis at 1.19-1.36 A resolution Medicago truncatula
3.1.3.25 structures of complexes with L-histidinol 1-phosphate, L-histidinol, and phosphate as well as the structure showing the cross-linking between two enzyme molecules. The enzymatic reaction requires Mg2+ cations and is catalyzed mainly by amino acid residues from the N-terminal domain. The C-terminal domain is responsible for the substrate specificity Medicago truncatula

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.15 T151A site-directed mutagenesis, inactive mutant Medicago truncatula

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.15 Li+ slight inhibition Medicago truncatula
3.1.3.25 CO2 enzyme dimers in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys158 and Cys245 residues Medicago truncatula
3.1.3.25 formaldehyde enzyme dimers in the presence of CO2 or formaldehyde form mutual, methylene-bridged cross-links between Lys158 and Cys245 residues Medicago truncatula
3.1.3.25 Li+
-
 Medicago truncatula

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.15 additional information
-
 additional information Michaelis-Menten kinetics Medicago truncatula
3.1.3.15 0.263
-
 L-histidinol phosphate pH 8.4, 22°C Medicago truncatula
3.1.3.25 0.263
-
 L-histidinol phosphate pH 8.4, 23°C Medicago truncatula

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.15 Mg2+ required for activity, best at 5 mM Medicago truncatula
3.1.3.25 Mg2+ required, optimum concentration 5 mM Medicago truncatula

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.15 61358
-
 dimer, mass spectrometry Medicago truncatula

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.15 L-histidinol phosphate + H2O Medicago truncatula
-
 L-histidinol + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.15 Medicago truncatula G7J7Q5 Medicago tribuloides
-
3.1.3.25 Medicago truncatula G7J7Q5
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.25 proteolytic modification sequence contains a N-terminal signal peptide. The cleavage is predicted to occur between Arg51 and Ala52 Medicago truncatula

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.15 L-histidinol phosphate + H2O
-
 Medicago truncatula L-histidinol + phosphate
-
 ?
3.1.3.25 L-histidinol phosphate + H2O
-
 Medicago truncatula L-histidinol + phosphate
-
 ?
3.1.3.25 additional information no substrate: D-myo-inositol-1-phosphate Medicago truncatula ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.15 dimer 2 * 30378, recombinant enzyme, mass spectrometry, the monomer is with the N-terminal SNA linker that resides after cleavage with tobacco etch virus protease, plus the difference from the two added methylene groups (24 Da) with SNAMSS adduct (577.6 Da) that most probably is an artifact resulting from the MS experiment Medicago truncatula
3.1.3.15 More covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds Medicago truncatula

Synonyms

EC Number Synonyms Comment Organism
3.1.3.15 11419457 locus name Medicago truncatula
3.1.3.15 histidinol phosphate phosphatase
-
 Medicago truncatula
3.1.3.15 HOLP
-
 Medicago truncatula
3.1.3.15 IMPase-like HPP
-
 Medicago truncatula
3.1.3.15 MtHPP
-
 Medicago truncatula
3.1.3.25 11419457
-
 Medicago truncatula

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.15 22
-
 assay at room temperature Medicago truncatula

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.15 3.6
-
 L-histidinol phosphate pH 8.4, 22°C Medicago truncatula
3.1.3.25 3.6
-
 L-histidinol phosphate pH 8.4, 23°C Medicago truncatula

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.15 8.4
-
-
 Medicago truncatula
3.1.3.25 8.4
-
-
 Medicago truncatula

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.1.3.15 5.5
-
 pH 8.4, 22°C Medicago truncatula Li+
3.1.3.25 5.5
-
 pH 8.4, 23°C Medicago truncatula Li+

General Information

EC Number General Information Comment Organism
3.1.3.15 additional information the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview Medicago truncatula
3.1.3.15 physiological function IMPase-like HPPs play a role only in His biosynthesis Medicago truncatula

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.3.15 13.69
-
 L-histidinol phosphate pH 8.4, 22°C Medicago truncatula
3.1.3.25 13.7
-
 L-histidinol phosphate pH 8.4, 23°C Medicago truncatula