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Literature summary for 3.7.1.18 extracted from

  • Grogan, G.; Roberts, G.A.; Bougioukou, D.; Turner, N.J.; Flitsch, S.L.
    The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily (2001), J. Biol. Chem., 276, 12565-12572.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
EDTA 119% activity at 1 mM Rhodococcus sp.
additional information the enzyme displays 25% higher activity in 50 mM phosphate buffer than 50 mM Tris/HCl at the same pH Rhodococcus sp.

Cloned(Commentary)

Cloned (Comment) Organism
gene camK, cloning and expression in Escherichia coli XL1 Blue Rhodococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
4-hydroxymercuribenzoate 14% inhibition at 1 mM Rhodococcus sp.
Cu2+ 72% inhibition at 1 mM Rhodococcus sp.
Hg2+ 98% inhibition at 1 mM Rhodococcus sp.
N-ethylmaleimide 68% inhibition at 1 mM Rhodococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
6-oxocamphor pH 7.0, 25°C Rhodococcus sp.

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Zn2+ has a poor influence on enzyme activity, no effect by 1 M NaCl Rhodococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28488
-
3 * 28488, mass spectrometry Rhodococcus sp.
83000
-
gel filtration Rhodococcus sp.

Organism

Organism UniProt Comment Textmining
Rhodococcus sp. Q93TU6 gene camK
-
Rhodococcus sp. NCIMB 9784 Q93TU6 gene camK
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 35.7fold from strain NCIMB 9784 Rhodococcus sp.

Source Tissue

Source Tissue Comment Organism Textmining
cell culture strain NCIMB 9784 is grown on (1R)-(+)-camphor as the sole carbon source Rhodococcus sp.
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
357.5
-
purified native enzyme, substrate 6-oxocamphor, pH 7.0, 25°C Rhodococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-oxocamphor + H2O the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview Rhodococcus sp. (2R,4S)-alpha-campholinic acid
-
?
6-oxocamphor + H2O the 6-oxocamphor hydrolase catalyzes the desymmetrization of 6-oxocamphor to yield (2R,4S)-alpha-campholinic acid, putative asymmetric hydrolysis mechanism for 6-oxocamphor hydrolase based on sequence homology and the known mechanism of the crotonase enzymes, overview Rhodococcus sp. NCIMB 9784 (2R,4S)-alpha-campholinic acid
-
?

Subunits

Subunits Comment Organism
trimer 3 * 28488, mass spectrometry Rhodococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rhodococcus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
167
-
6-oxocamphor pH 7.0, 25°C Rhodococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Rhodococcus sp.

pI Value

Organism Comment pI Value Maximum pI Value
Rhodococcus sp. isoelectric focusing
-
8.5

General Information

General Information Comment Organism
evolution the enzyme belongs to the TetR/AcrR family of the crotonase superfamily Rhodococcus sp.