Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.7.1.18 EDTA 119% activity at 1 mM Rhodococcus sp.
3.7.1.18 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.7.1.18 4-hydroxymercuribenzoate 14% inhibition at 1 mM Rhodococcus sp.
3.7.1.18 Cu2+ 72% inhibition at 1 mM Rhodococcus sp.
3.7.1.18 Hg2+ 98% inhibition at 1 mM Rhodococcus sp.
3.7.1.18 N-ethylmaleimide 68% inhibition at 1 mM Rhodococcus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.7.1.18 0.05
-
 6-oxocamphor pH 7.0, 25°C Rhodococcus sp.

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.7.1.18 28488
-
 3 * 28488, mass spectrometry Rhodococcus sp.
3.7.1.18 83000
-
 gel filtration Rhodococcus sp.

Organism

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

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.7.1.18 357.5
-
 purified native enzyme, substrate 6-oxocamphor, pH 7.0, 25°C Rhodococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.7.1.18 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
-
 ?
3.7.1.18 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.7.1.18 25
-
 assay at Rhodococcus sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7.1.18 167
-
 6-oxocamphor pH 7.0, 25°C Rhodococcus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.7.1.18 7
-
 assay at Rhodococcus sp.

pI Value

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

General Information

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