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Literature summary for 3.1.3.15 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)

Crystallization (Comment) Organism
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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
Li+ slight inhibition Medicago truncatula

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity, best at 5 mM Medicago truncatula

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Medicago truncatula G7J7Q5 Medicago tribuloides
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidinol phosphate + H2O
-
Medicago truncatula L-histidinol + phosphate
-
?

Subunits

Subunits Comment Organism
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
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

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
-
Medicago truncatula

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
5.5
-
pH 8.4, 22°C Medicago truncatula Li+

General Information

General Information Comment Organism
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
physiological function IMPase-like HPPs play a role only in His biosynthesis Medicago truncatula

kcat/KM [mM/s]

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