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Literature summary for 3.1.3.15 extracted from

  • Ghodge, S.V.; Fedorov, A.A.; Fedorov, E.V.; Hillerich, B.; Seidel, R.; Almo, S.C.; Raushel, F.M.
    Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins (2013), Biochemistry, 52, 1101-1112.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.15

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Lactococcus lactis subsp. lactis

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 25% (w/v) PEG 4000, 0.1 M sodium acetate (pH 4.6), and 0.2 M ammonium sulfate Lactococcus lactis subsp. lactis

Protein Variants

Protein Variants Comment Organism
D17N inactive Lactococcus lactis subsp. lactis
D228N the mutant shows reduced catalytic efficiency and kcat is reduced by approximately 6000fold compared to the wild type enzyme Lactococcus lactis subsp. lactis
E115Q the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
H230N inactive Lactococcus lactis subsp. lactis
H42N the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
R160A inactive Lactococcus lactis subsp. lactis
R197M the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
Y117A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
Y117F the mutant shows increased catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
Y157F the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
Y161A the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis
Y161F the mutant shows reduced catalytic efficiency compared to the wild type enzyme Lactococcus lactis subsp. lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
 L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
0.74
-
 L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
1.3
-
 L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
1.5
-
 L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
1.7
-
 L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
1.7
-
 L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
1.9
-
 L-histidinol phosphate wild type enzyme, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
2.3
-
 L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
2.5
-
 L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
4.5
-
 L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
5.4
-
 L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron contains iron in the active site Lactococcus lactis subsp. lactis
additional information the enzyme does not show any significant increases in catalytic activity when Zn2+, Mn2+, Co2+ or Ni2+ are added Lactococcus lactis subsp. lactis
Zn2+ contains Zn2+ in the active site Lactococcus lactis subsp. lactis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-histidinol phosphate + H2O Lactococcus lactis subsp. lactis
-
 L-histidinol + phosphate
-
 ?
L-histidinol phosphate + H2O Lactococcus lactis subsp. lactis IL1403
-
 L-histidinol + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Lactococcus lactis subsp. lactis Q02150
-
-
Lactococcus lactis subsp. lactis IL1403 Q02150
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity chromatography Lactococcus lactis subsp. lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidinol phosphate + H2O
-
 Lactococcus lactis subsp. lactis L-histidinol + phosphate
-
 ?
L-histidinol phosphate + H2O
-
 Lactococcus lactis subsp. lactis IL1403 L-histidinol + phosphate
-
 ?
N-formyl-L-histidinol phosphate + H2O the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5 Lactococcus lactis subsp. lactis N-formyl-L-histidinol + phosphate
-
 ?
N-formyl-L-histidinol phosphate + H2O the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5 Lactococcus lactis subsp. lactis IL1403 N-formyl-L-histidinol + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
HPP
-
 Lactococcus lactis subsp. lactis
L-histidinol phosphate phosphatase
-
 Lactococcus lactis subsp. lactis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.031
-
 L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
0.62
-
 L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
0.74
-
 L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
31
-
 L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
38
-
 L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
48
-
 L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
53
-
 L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
61
-
 L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
110
-
 L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
174
-
 L-histidinol phosphate wild type enzyme, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
180
-
 L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.22
-
 L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
0.48
-
 L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
0.49
-
 L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
8.5
-
 L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
9.8
-
 L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
18
-
 L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
25
-
 L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
36
-
 L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
79
-
 L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
89
-
 L-histidinol phosphate at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
150
-
 L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis