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Literature summary for 4.2.1.53 extracted from

  • Bevers, L.E.; Pinkse, M.W.; Verhaert, P.D.; Hagen, W.R.
    Oleate hydratase catalyzes the hydration of a nonactivated carbon-carbon bond (2009), J. Bacteriol., 191, 5010-5012.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.53

Activating Compound

Activating Compound Comment Organism Structure
additional information addition of EDTA or EGTA (both at a 1000fold excess) has no effect on the activity Elizabethkingia meningoseptica

Cloned(Commentary)

Cloned (Comment) Organism
into the pBAD/His A vector and expressed in Escherichia coli TOP10 cells Elizabethkingia meningoseptica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.078
-
 oleic acid at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm, in the presence of 2.5% isopropyl alcoho Elizabethkingia meningoseptica
0.121
-
 oleic acid at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm Elizabethkingia meningoseptica
0.21
-
 oleic acid at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1000 rpm Elizabethkingia meningoseptica
0.3
-
 oleic acid at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm Elizabethkingia meningoseptica
0.56
-
 oleic acid at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm Elizabethkingia meningoseptica

Metals/Ions

Metals/Ions Comment Organism Structure
additional information calcium has no role in the catalytic mechanism Elizabethkingia meningoseptica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 gel filtration Elizabethkingia meningoseptica
73487
-
 1 * 73487, calculated from sequence Elizabethkingia meningoseptica

Organism

Organism UniProt Comment Textmining
Elizabethkingia meningoseptica C7DLJ6 formerly Pseudomonas sp. strain 3266
-

Purification (Commentary)

Purification (Comment) Organism
by three steps of gel filtration. Recombinant oleate hydratase fused to an N-terminal His tag purified onh Ni-resin Elizabethkingia meningoseptica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activity of the enzyme does not change significantly in the presence of 2.5% or 5% isopropyl alcohol, but it decreases at isopropyl alcohol concentrations higher than 10% Elizabethkingia meningoseptica
0.14
-
 at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm Elizabethkingia meningoseptica
0.16
-
 at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm Elizabethkingia meningoseptica
0.17
-
 at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1000 rpm Elizabethkingia meningoseptica
0.34
-
 at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm, in the presence of 2.5% isopropyl alcohol Elizabethkingia meningoseptica
0.39
-
 at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm Elizabethkingia meningoseptica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oleic acid + H2O
-
 Elizabethkingia meningoseptica 10-hydroxystearic acid
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 73487, calculated from sequence Elizabethkingia meningoseptica

Synonyms

Synonyms Comment Organism
OA hydratase
-
 Elizabethkingia meningoseptica
oleate hydratase
-
 Elizabethkingia meningoseptica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Elizabethkingia meningoseptica

pH Range

pH Minimum pH Maximum Comment Organism
5 7 pH 5: about 70% of maximal activity, pH 7: about about 75% of maximal activity Elizabethkingia meningoseptica

Expression

Organism Comment Expression
Elizabethkingia meningoseptica expression is strongly upregulated in cells grown in the presence of oleic acid up