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Literature summary for 3.1.3.15 extracted from

  • Rangarajan, E.S.; Proteau, A.; Wagner, J.; Hung, M.N.; Matte, A.; Cygler, M.
    Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway (2006), J. Biol. Chem., 281, 37930-37941.
    View publication on PubMed
Search for more literature for 3.1.3.15

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
25% (w/v) polyethylene glycol 3350, 0.2M MgCl2 and 0.1 M Tris-HCl (pH 8.5) by the sitting drop vapor diffusion, or 30% (w/v) polyethylene glycol monomethyl ether, 0.05 M CaCl2, and 0.1 M Bis-Tris (pH 6.5) by the micro-batch method Escherichia coli

Protein Variants

Protein Variants Comment Organism
D12A shows only traces of the wild type activity Escherichia coli
E18A shows about 5% of the wild-type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 0.1 mM, no activity Escherichia coli
EDTA 0.1 mM, no activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.041
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+ Escherichia coli
0.052
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+ Escherichia coli
0.054
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+ Escherichia coli
0.054
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activating Escherichia coli
Mn2+ activating Escherichia coli
Zn2+ activating Escherichia coli
Zn2+ the presence of a structural Zn2+ ion stabilizes the conformation of an extended loop Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
19903
-
 2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel-nitrilotriacetic acid column chromatography Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry Escherichia coli

Synonyms

Synonyms Comment Organism
HisB-N N-terminal domain of the bifunctional enzyme HisB with histidinol phosphate phosphatase activity Escherichia coli
histidinol phosphate phosphatase
-
 Escherichia coli
HPase
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20 50 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+ Escherichia coli
960
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+ Escherichia coli
1410
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+ Escherichia coli
2140
-
 L-histidinol phosphate in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+ Escherichia coli