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Literature summary for 1.14.11.55 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
Search for more literature for 1.14.11.55

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Virgibacillus salexigens Q2TDY4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ectoine + 2-oxoglutarate + O2
-
 Virgibacillus salexigens 5-hydroxyectoine + succinate + CO2
-
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