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Literature summary extracted from

  • Widderich, N.; Pittelkow, M.; Hoeppner, A.; Mulnaes, D.; Buckel, W.; Gohlke, H.; Smits, S.H.; Bremer, E.
    Molecular dynamics simulations and structure-guided mutagenesis provide insight into the architecture of the catalytic core of the ectoine hydroxylase (2014), J. Mol. Biol., 426, 586-600.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.55 structural comparison, molecular dynamics simulations, and site-directed mutagenesis suggest the positioning of the iron, ectoine, and 2-oxoglutarate ligands in close proximity to each other and with a spatial orientation that will allow the region-selective and stereo-specific hydroxylation of (4S)-ectoine to (4S,5S)-5-hydroxyectoine Virgibacillus salexigens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.55 A163C residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 A163C/S244C residues are not involved in ligand binding Virgibacillus salexigens
1.14.11.55 D148A loss of activity. Residue is involved in binding of Fe2+ Virgibacillus salexigens
1.14.11.55 D148E loss of activity. Residue is involved in binding of Fe2+ Virgibacillus salexigens
1.14.11.55 F143A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 F143W loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 F143Y loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 F242A loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 F242W loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 F242Y 3fold increase in Km value Virgibacillus salexigens
1.14.11.55 F263A loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 F263W loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 F263Y 30% increase in Km value Virgibacillus salexigens
1.14.11.55 F95A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 H146A loss of activity. Residue is involved in binding of Fe2+ Virgibacillus salexigens
1.14.11.55 H248A loss of activity. Residue is involved in binding of Fe2+ Virgibacillus salexigens
1.14.11.55 N133A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 N261A residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 P198A activity similar to wild-type, residue of loop region Virgibacillus salexigens
1.14.11.55 Q129A loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 R131A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 R259A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 R259H loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 R259K loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 R259Q loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 S165A 3fold increase in Km value Virgibacillus salexigens
1.14.11.55 S167A residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 S205A activity similar to wild-type, residue of loop region Virgibacillus salexigens
1.14.11.55 S244C residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 S250A loss of activity. Residue is involved in binding of 2-oxoglutarate Virgibacillus salexigens
1.14.11.55 V265A residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 V265L residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 V265T residue is not involved in ligand binding Virgibacillus salexigens
1.14.11.55 W152A loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 W152F loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens
1.14.11.55 W152Y loss of activity. Residue is involved in binding of ectoine Virgibacillus salexigens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.11.55 5.9
-
 ectoine wild-type, pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 6.8
-
 ectoine mutant S205A, pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 7.1
-
 ectoine mutant P198A, pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 8
-
 ectoine mutant F263Y, pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 17.3
-
 ectoine mutant S165A, pH 7.5, 32°C Virgibacillus salexigens
1.14.11.55 19.6
-
 ectoine mutant F242Y, pH 7.5, 32°C Virgibacillus salexigens

Organism

EC Number Organism UniProt Comment Textmining
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
-
 Virgibacillus salexigens 5-hydroxyectoine + succinate + CO2
-
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