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

BRENDA support

4.1.3.36: 1,4-dihydroxy-2-naphthoyl-CoA synthase

This is an abbreviated version!
For detailed information about 1,4-dihydroxy-2-naphthoyl-CoA synthase, go to the full flat file.

Word Map on EC 4.1.3.36

Reaction

4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
=
1,4-dihydroxy-2-naphthoyl-CoA
+
H2O

Synonyms

1,4-dihydroxy-2-naphthoate synthetase, 1,4-dihydroxy-2-naphthoyl coenzyme A synthase, 1,4-dihydroxy-2-naphthoyl-CoA synthase, 1,4-dihydroxy-2-naphthoyl-coenzyme synthase, DHNA synthetase, DHNA-CoA synthase, dihydroxynaphthoate synthase, Dihydroxynaphthoic acid synthetase, MenB, naphthoate synthase, naphthoate synthase (MenB), Rv0548c, synthase, 1,4-dihydroxy-2-naphthoate

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.36 1,4-dihydroxy-2-naphthoyl-CoA synthase

Crystallization

Crystallization on EC 4.1.3.36 - 1,4-dihydroxy-2-naphthoyl-CoA synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme free or in complex with bicarbonate or nitrate, hanging drop vapor diffusion method, 0.01 ml of protein solution containing 10 mg/mL purified ecMenB, 25 mM Tris, pH 8.0, and 10% glycerol, including 10 mM NaHCO3 or NaNO3 for the complexed enzyme, is mixed with 0.001 ml of reservoir solution containing reservoir solution containing 300 mM NaCl, 100 mM Tris, pH 7.5, 2% Tacsimate, and 20% PEG 335, equilibration against 0.5 ml of reservoir solution, 22°C, X-ray diffraction structure determination and analysis at 2.30 A resolution
-
purified recombinant enzyme, hanging drop method, mixing of protein solution containing 10 mg/ml protein in 10 mM NaHCO3, 10 mM 1-hydroxy-2-naphthoyl-CoA, and 25 mM Tris, pH 8.0, with reservoir solution containing 200 mM (NH4)2SO4 and 23% PEG 3,350 in 100 mM Bis-Tris, pH 5.5, in a 1:1 ratio, 1 week, X-ray diffraction structure determination and analysis at 1.84 A resolution
-
sitting drop vapor diffusion technique, PEG 3350, in complex with o-succinylbenzoyl-amino-CoA
-
sitting drop vapour diffusion method with 30% (v/v) pentaerythritol ethocylate, 0.05 M ammonium sulfate, and 0.05 M bis-Tris pH 6.5
-
hanging drop vapor diffusion technique, PEG 6000, in complex with o-succinylbenzoyl-aminoCoA
in complex with 1-hydroxy-2-naphthoyl-CoA or salicylyl-CoA, hanging drop vapor diffusion method, using 0.3 M NaCl, 0.1 M Tris-HCl pH 8.0, 25% (w/v) PEG 3350
sitting-drop or hanging-drop vapour-diffusion method, structure of native enzyme determined at 2.15 A resolution and structure of the naphthoyl-CoA complex is determined at 2.3 A resolution
sitting drop vapour diffusion method with 0.1 M NaHEPES pH 7.5, 1.6 M ammonium sulfate, 0.2 M NaCl
purified recombinant enzyme, hanging drop method, mixing of protein solution containing 10 mg/ml protein in 10 mM NaHCO3, 5 mM 1-hydroxy-2-naphthoyl-CoA, 5 mM salicyloyl-CoA, 20 mM glycine, pH 9.75, 1% glycerol, and 10 mM NaHCO3 or 0.15 M ammonium acetate, 4% tacsimate, 15% PEG 3350, and 100 mM Bis-Tris, pH 6.0, with reservoir solution containing 0.15 M ammonium acetate, 0.3 M ammonium sulfate, 16% PEG 3350, 100 mM Bis-Tris, pH 5.7, and 10 mM proline or 10 mM taurine, in a 1:1 ratio, 1 week, X-ray diffraction structure determination and analysis at 2.0-2.35 A resolution
purified recombinant enzyme, hanging drop vapor diffusion method, 0.01 ml of protein solution containing 10 mg/mL purified scMenB, 20 mM glycine, pH 9.75, and 1% glycerol, with or without 10 mM NaHCO3, is mixed with 0.001 ml of reservoir solution containing of 0.15 M ammonium acetate, 0.02 M L-proline, 0.1 M Bis-Tris, pH 6.1, and 45% MPD, equilibration against 0.5 ml of reservoir solution, 22°C, X-ray diffraction structure determination and analysis at 2.04 A resolution