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Literature summary extracted from

  • Widderich, N.; Hoeppner, A.; Pittelkow, M.; Heider, J.; Smits, S.H.; Bremer, E.
    Biochemical properties of ectoine hydroxylases from extremophiles and their wider taxonomic distribution among microorganisms (2014), PLoS ONE, 9, e93809.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.55 to 1.9 A resolution, and comparison of iron-bound and apo structure. The iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Virgibacillus salexigens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.11.55 NaCl maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory Acidiphilium cryptum
1.14.11.55 NaCl maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory Alkalilimnicola ehrlichii
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Halomonas elongata
1.14.11.55 NaCl maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory Paenibacillus lautus
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Pseudomonas stutzeri
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Sphingopyxis alaskensis
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Virgibacillus salexigens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.55 2.7
-
 2-oxoglutarate pH 7.5, 32°C Sphingopyxis alaskensis
1.14.11.55 3.9
-
 2-oxoglutarate pH 7.5, 32°C Paenibacillus lautus
1.14.11.55 4.1
-
 2-oxoglutarate pH 7.5, 32°C Acidiphilium cryptum
1.14.11.55 4.6
-
 2-oxoglutarate pH 7.5, 32°C Pseudomonas stutzeri
1.14.11.55 4.8
-
 2-oxoglutarate pH 7.5, 32°C Halomonas elongata
1.14.11.55 4.9
-
 2-oxoglutarate pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 5
-
 2-oxoglutarate pH 7.5, 32°C Alkalilimnicola ehrlichii
1.14.11.55 5.7
-
 ectoine pH 7.5, 32°C Halomonas elongata
1.14.11.55 5.9
-
 ectoine pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 6.2
-
 ectoine pH 7.5, 32°C Pseudomonas stutzeri
1.14.11.55 9
-
 ectoine pH 7.5, 32°C Alkalilimnicola ehrlichii
1.14.11.55 9.5
-
 ectoine pH 7.5, 32°C Paenibacillus lautus
1.14.11.55 9.8
-
 ectoine pH 7.5, 32°C Sphingopyxis alaskensis
1.14.11.55 10
-
 ectoine pH 7.5, 32°C Acidiphilium cryptum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Pseudomonas stutzeri
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Virgibacillus salexigens
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Sphingopyxis alaskensis
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Halomonas elongata
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Paenibacillus lautus
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Alkalilimnicola ehrlichii
1.14.11.55 Iron the iron ligand is bound via interaction with histidine side-chains His146 and His248, and the side-chain of Asp-148. These residues form a conserved H6D/E…H motif, the so-called 2-His-1-carboxylate facial triad Acidiphilium cryptum
1.14.11.55 KCl maximum activity in presence of 100 mM KCl Sphingopyxis alaskensis
1.14.11.55 KCl maximum activity in presence of 100 mM KCl Acidiphilium cryptum
1.14.11.55 KCl maximum activity in presence of 150 mM KCl Pseudomonas stutzeri
1.14.11.55 KCl maximum activity in presence of 150 mM KCl Virgibacillus salexigens
1.14.11.55 KCl maximum activity in presence of 150 mM KCl Halomonas elongata
1.14.11.55 KCl maximum activity in presence of 150 mM KCl Alkalilimnicola ehrlichii
1.14.11.55 KCl maximum activity in presence of 200 mM KCl Paenibacillus lautus
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Pseudomonas stutzeri
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Virgibacillus salexigens
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Sphingopyxis alaskensis
1.14.11.55 NaCl maximum activity in presence of 100 mM KCl. High concentrations of NaCl are inhibitory Halomonas elongata
1.14.11.55 NaCl maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory Paenibacillus lautus
1.14.11.55 NaCl maximum activity in presence of 150 mM KCl. High concentrations of NaCl are inhibitory Alkalilimnicola ehrlichii
1.14.11.55 NaCl maximum activity in presence of 50 mM KCl. High concentrations of NaCl are inhibitory Acidiphilium cryptum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.11.55 34100
-
-
 Sphingopyxis alaskensis
1.14.11.55 34100
-
-
 Acidiphilium cryptum
1.14.11.55 34200
-
 x * 34200, SDS-PAGE Pseudomonas stutzeri
1.14.11.55 34300
-
 x * 34300, SDS-PAGE Alkalilimnicola ehrlichii
1.14.11.55 34400
-
 x * 34400, SDS-PAGE Virgibacillus salexigens
1.14.11.55 34800
-
 x * 34800, SDS-PAGE Paenibacillus lautus
1.14.11.55 37400
-
-
 Halomonas elongata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.55 ectoine + 2-oxoglutarate + O2 Pseudomonas stutzeri
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Virgibacillus salexigens
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Sphingopyxis alaskensis
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Halomonas elongata
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Paenibacillus lautus
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Alkalilimnicola ehrlichii
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Acidiphilium cryptum
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Pseudomonas stutzeri A1501
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Sphingopyxis alaskensis DSM 13593
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2 Halomonas elongata DSM 2581
-
 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 additional information Pseudomonas stutzeri ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Virgibacillus salexigens ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Sphingopyxis alaskensis ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Halomonas elongata ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Paenibacillus lautus ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Alkalilimnicola ehrlichii ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Acidiphilium cryptum ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Pseudomonas stutzeri A1501 ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Sphingopyxis alaskensis DSM 13593 ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?
1.14.11.55 additional information Halomonas elongata DSM 2581 ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.55 Acidiphilium cryptum JN019030 ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55 Alkalilimnicola ehrlichii JN019031 ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55 Halomonas elongata E1VA04
-
-
1.14.11.55 Halomonas elongata DSM 2581 E1VA04
-
-
1.14.11.55 Paenibacillus lautus A0A1R1AUM9 ectD gene optimized for the expression in Escherichia coli
-
1.14.11.55 Pseudomonas stutzeri
-
-
-
1.14.11.55 Pseudomonas stutzeri A1501
-
-
-
1.14.11.55 Sphingopyxis alaskensis Q1GNW5
-
-
1.14.11.55 Sphingopyxis alaskensis DSM 13593 Q1GNW5
-
-
1.14.11.55 Virgibacillus salexigens Q2TDY4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Pseudomonas stutzeri 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Virgibacillus salexigens 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Sphingopyxis alaskensis 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Halomonas elongata 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Paenibacillus lautus 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Alkalilimnicola ehrlichii 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Acidiphilium cryptum 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Pseudomonas stutzeri A1501 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Sphingopyxis alaskensis DSM 13593 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 ectoine + 2-oxoglutarate + O2
-
 Halomonas elongata DSM 2581 5-hydroxyectoine + succinate + CO2
-
 ir
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Pseudomonas stutzeri ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Virgibacillus salexigens ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Sphingopyxis alaskensis ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Halomonas elongata ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Paenibacillus lautus ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Alkalilimnicola ehrlichii ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Acidiphilium cryptum ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Pseudomonas stutzeri A1501 ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Sphingopyxis alaskensis DSM 13593 ?
-
 ?
1.14.11.55 additional information ectoine hydroxylase operates exclusively in one direction under physiologically relevant conditions to direct the formation of 5-hydroxyectoine from the precursor ectoine Halomonas elongata DSM 2581 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.11.55 ? x * 34200, SDS-PAGE Pseudomonas stutzeri
1.14.11.55 ? x * 34400, SDS-PAGE Virgibacillus salexigens
1.14.11.55 ? x * 34800, SDS-PAGE Paenibacillus lautus
1.14.11.55 ? x * 34300, SDS-PAGE Alkalilimnicola ehrlichii
1.14.11.55 ? x * 34100, SDS-PAGE Sphingopyxis alaskensis
1.14.11.55 ? x * 34100, SDS-PAGE Acidiphilium cryptum
1.14.11.55 ? x * 37400, SDS-PAGE Halomonas elongata

Synonyms

EC Number Synonyms Comment Organism
1.14.11.55 ectD
-
 Pseudomonas stutzeri
1.14.11.55 ectD
-
 Virgibacillus salexigens
1.14.11.55 ectD
-
 Sphingopyxis alaskensis
1.14.11.55 ectD
-
 Halomonas elongata
1.14.11.55 ectD
-
 Paenibacillus lautus
1.14.11.55 ectD
-
 Alkalilimnicola ehrlichii
1.14.11.55 ectD
-
 Acidiphilium cryptum
1.14.11.55 Sala_2952
-
 Sphingopyxis alaskensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.11.55 32
-
-
 Virgibacillus salexigens
1.14.11.55 32
-
-
 Halomonas elongata
1.14.11.55 32
-
-
 Acidiphilium cryptum
1.14.11.55 35
-
-
 Pseudomonas stutzeri
1.14.11.55 35
-
-
 Alkalilimnicola ehrlichii
1.14.11.55 40
-
-
 Sphingopyxis alaskensis
1.14.11.55 40
-
-
 Paenibacillus lautus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.14.11.55 5 50
-
 Virgibacillus salexigens
1.14.11.55 5 50
-
 Sphingopyxis alaskensis
1.14.11.55 5 47
-
 Halomonas elongata
1.14.11.55 10 50
-
 Pseudomonas stutzeri
1.14.11.55 10 47
-
 Acidiphilium cryptum
1.14.11.55 15 50
-
 Paenibacillus lautus
1.14.11.55 15 45
-
 Alkalilimnicola ehrlichii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.11.55 1.2
-
 ectoine pH 7.5, 32°C Sphingopyxis alaskensis
1.14.11.55 1.2
-
 ectoine pH 7.5, 32°C Alkalilimnicola ehrlichii
1.14.11.55 1.6
-
 ectoine pH 7.5, 32°C Paenibacillus lautus
1.14.11.55 2.8
-
 ectoine pH 7.5, 32°C Halomonas elongata
1.14.11.55 3.4
-
 ectoine pH 7.5, 32°C Acidiphilium cryptum
1.14.11.55 7.7
-
 ectoine pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 8.9
-
 ectoine pH 7.5, 32°C Pseudomonas stutzeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.11.55 7.5
-
-
 Pseudomonas stutzeri
1.14.11.55 7.5
-
-
 Virgibacillus salexigens
1.14.11.55 7.5
-
-
 Paenibacillus lautus
1.14.11.55 7.5
-
-
 Alkalilimnicola ehrlichii
1.14.11.55 8
-
-
 Sphingopyxis alaskensis
1.14.11.55 8
-
-
 Halomonas elongata
1.14.11.55 8
-
-
 Acidiphilium cryptum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.11.55 5.5 9.6
-
 Pseudomonas stutzeri
1.14.11.55 5.5 9.6
-
 Virgibacillus salexigens
1.14.11.55 5.5 9.6
-
 Sphingopyxis alaskensis
1.14.11.55 5.5 9.6
-
 Paenibacillus lautus
1.14.11.55 5.5 9.6
-
 Acidiphilium cryptum
1.14.11.55 6.5 9.6
-
 Halomonas elongata
1.14.11.55 6.5 9.6
-
 Alkalilimnicola ehrlichii

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.14.11.55 Pseudomonas stutzeri calculated
-
 5.5
1.14.11.55 Sphingopyxis alaskensis calculated
-
 5.5
1.14.11.55 Paenibacillus lautus calculated
-
 5.6
1.14.11.55 Alkalilimnicola ehrlichii calculated
-
 5.7
1.14.11.55 Virgibacillus salexigens calculated
-
 5.8
1.14.11.55 Halomonas elongata calculated
-
 5.8
1.14.11.55 Acidiphilium cryptum calculated
-
 5.8

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.11.55 0.12
-
 ectoine pH 7.5, 32°C Sphingopyxis alaskensis
1.14.11.55 0.13
-
 ectoine pH 7.5, 32°C Alkalilimnicola ehrlichii
1.14.11.55 0.17
-
 ectoine pH 7.5, 32°C Paenibacillus lautus
1.14.11.55 0.34
-
 ectoine pH 7.5, 32°C Acidiphilium cryptum
1.14.11.55 0.49
-
 ectoine pH 7.5, 32°C Halomonas elongata
1.14.11.55 1.31
-
 ectoine pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 1.44
-
 ectoine pH 7.5, 32°C Pseudomonas stutzeri