Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.15 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.15 0.14
-
L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 0.74
-
L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 1.3
-
L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 1.5
-
L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 1.7
-
L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 1.7
-
L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 1.9
-
L-histidinol phosphate wild type enzyme, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 2.3
-
L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 2.5
-
L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 4.5
-
L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 5.4
-
L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.15 Iron contains iron in the active site Lactococcus lactis subsp. lactis
3.1.3.15 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
3.1.3.15 Zn2+ contains Zn2+ in the active site Lactococcus lactis subsp. lactis

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 Lactococcus lactis subsp. lactis
-
L-histidinol + phosphate
-
?
3.1.3.15 L-histidinol phosphate + H2O Lactococcus lactis subsp. lactis IL1403
-
L-histidinol + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.15 Lactococcus lactis subsp. lactis Q02150
-
-
3.1.3.15 Lactococcus lactis subsp. lactis IL1403 Q02150
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.15 L-histidinol phosphate + H2O
-
Lactococcus lactis subsp. lactis L-histidinol + phosphate
-
?
3.1.3.15 L-histidinol phosphate + H2O
-
Lactococcus lactis subsp. lactis IL1403 L-histidinol + phosphate
-
?
3.1.3.15 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
-
?
3.1.3.15 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

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.15 0.031
-
L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 0.62
-
L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 0.74
-
L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 31
-
L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 38
-
L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 48
-
L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 53
-
L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 61
-
L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 110
-
L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 174
-
L-histidinol phosphate wild type enzyme, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 180
-
L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis

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 0.22
-
L-histidinol phosphate mutant enzyme D228N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 0.48
-
L-histidinol phosphate mutant enzyme H42N, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 0.49
-
L-histidinol phosphate mutant enzyme R160M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 8.5
-
L-histidinol phosphate mutant enzyme R197M, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 9.8
-
L-histidinol phosphate mutant enzyme Y117A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 18
-
L-histidinol phosphate mutant enzyme E115Q, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 25
-
L-histidinol phosphate mutant enzyme Y161A, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 36
-
L-histidinol phosphate mutant enzyme HY157F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 79
-
L-histidinol phosphate mutant enzyme Y161F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 89
-
L-histidinol phosphate at pH 9.0 and 22°C Lactococcus lactis subsp. lactis
3.1.3.15 150
-
L-histidinol phosphate mutant enzyme Y117F, at pH 9.0 and 22°C Lactococcus lactis subsp. lactis