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2-(3-carboxypropyl)-benzoyl-CoA
?
-
-
-
?
2-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
formation of a structural motif like an oxyanion hole for orientation of the o-succinylbenzoate substrate and stabilization of the oxyanion intermediate in the intramolecular Claisen condensation, which involves a conserved tyrosine residue in the A-loop. via induced fit
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
catalyzes an intramolecular Claisen condensation reaction leading to the formation of 1,4-dihydroxy-2-naphthoyl-CoA from o-succinylbenzoate, the enzyme substrate is chemically unstable
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
catalyzes an intramolecular Claisen condensation reaction leading to the formation of 1,4-dihydroxy-2-naphthoyl-CoA from o-succinylbenzoate, the enzyme substrate is chemically unstable
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
formation of a structural motif like an oxyanion hole for orientation of the o-succinylbenzoate substrate and stabilization of the oxyanion intermediate in the intramolecular Claisen condensation, which involves a conserved tyrosine residue in the A-loop via induced fit
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
highly specific, no substrates are 2-(3'-carboxypropionyl)benzoyl-CoA or 4-(2'-carboxyphenyl)4-oxobutyryl-diCoA
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
highly specific, no substrates are 2-(3'-carboxypropionyl)benzoyl-CoA or 4-(2'-carboxyphenyl)4-oxobutyryl-diCoA
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
highly specific, no substrates are 2-(3'-carboxypropionyl)benzoyl-CoA or 4-(2'-carboxyphenyl)4-oxobutyryl-diCoA
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
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o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
formation of a structural motif like an oxyanion hole for orientation of the o-succinylbenzoate substrate and stabilization of the oxyanion intermediate in the intramolecular Claisen condensation, which involves a conserved tyrosine residue in the A-loop. via induced fit
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoate + CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
formation of a structural motif like an oxyanion hole for orientation of the o-succinylbenzoate substrate and stabilization of the oxyanion intermediate in the intramolecular Claisen condensation, which involves a conserved tyrosine residue in the A-loop via induced fit
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
1,4-dihydroxy-2-naphthoyl-CoA + H2O
-
-
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
o-succinylbenzoyl-CoA
?
-
pathway in menaquinone biosynthesis, i.e. vitamin K2, cf. EC 6.2.1.26
-
-
?
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(3Z)-3-(3,3-dimethyl-2-oxobutylidene)-3,4-dihydro-2H-1,4-benzoxazin-2-one
-
68.4% inhibition at 0.125 mg/ml, 0.00015 mM o-succinylbenzoate , pH not specified in the publication, temperature not specified in the publication
(3Z)-3-(3,3-dimethyl-2-oxobutylidene)-6-(ethylsulfonyl)-3,4-dihydro-2H-1,4-benzoxazin-2-one
-
60.3% inhibition at 0.125 mg/ml, 0.00015 mM o-succinylbenzoate, pH not specified in the publication, temperature not specified in the publication
(3Z)-6-chloro-3-(4-methyl-2-oxopentylidene)-3,4-dihydro-2H-1,4-benzoxazin-2-one
-
98% inhibition at 0.125 mg/ml, 0.00015 mM o-succinylbenzoate, pH not specified in the publication, temperature not specified in the publication
(3Z)-6-methyl-3-(4-methyl-2-oxopentylidene)-3,4-dihydro-2H-1,4-benzoxazin-2-one
-
77.3% inhibition at 0.125 mg/ml, 0.00015 mM o-succinylbenzoate, pH not specified in the publication, temperature not specified in the publication
1-hydroxy-2-naphthoyl-CoA
2,3-dihydroxybenzoyl-CoA
-
-
2,4-dihydroxybenzoyl-CoA
-
-
2-CoA-4-(2,4-dichlorophenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-bromophenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-chlorophenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-fluorophenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-iodophenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-methoxyphenyl)-4-oxobutanoic acid
-
2-CoA-4-(2-nitrophenyl)-4-oxobutanoic acid
-
2-CoA-4-(3-chlorophenyl)-4-oxobutanoic acid
-
2-CoA-4-(4-dichlorophenyl)-4-oxobutanoic acid
-
2-CoA-4-(4-methoxyphenyl)-4-oxobutanoic acid
-
3-(2,4-dichlorophenyl)-3-oxopropyl-CoA
weak inhibition
4-(2,4-dichlorophenyl)-4-oxobutanoyl-CoA
-
4-(2-chlorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
half-life at 25°C, pH 7.4, is 0.4 h
4-(2-methoxyphenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
half-life at 25°C, pH 7.4, is 11.6 h
4-(4-chlorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
half-life at 25°C, pH 7.4, is 6.8 h
4-(4-fluorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
half-life at 25°C, pH 7.4, is 12.2 h
4-oxo-2-[[(1S)-1-phenylethyl]amino]-4-[2-(trifluoromethyl)phenyl]butanoic acid
half-life at 25°C, pH 7.4, is 0.2 h
4-oxo-4-chlorophenylbutenoyl methyl ester
penetrates the cell where it is hydrolyzed and reacts with CoA to generate the active antibacterial compound, mechanism, overview
4-oxo-4-phenyl-2-[[(1S)-1-phenylethyl]amino]butanoic acid
half-life at 25°C, pH 7.4, is 11.6 h
adenosine 5'-propylphosphate
-
-
methyl (2Z)-(2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(5-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(6-chloro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(6-fluoro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(6-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(6-nitro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(7-chloro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(7-fluoro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(7-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-(7-nitro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
-
-
methyl (2Z)-[6-(ethylsulfonyl)-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene]ethanoate
-
-
O5'-(4-(3-[2-[2-((R)-3-hydroxy-4-(trimethylammonio)-1-oxo-butyl)sulfanyl-ethylcarbamoyl]-ethylcarbamoyl]-(R)-3-hydroxy-2,2-dimethyl-propyl)-1-hydroxy-3-oxido-1,3-dioxo-2,4-dioxa-1,3-diphosphabut-1-yl) 3'-phospho-adenosine
-
-
oxidized coenzyme A
-
-
-
1-hydroxy-2-naphthoyl-CoA
-
-
1-hydroxy-2-naphthoyl-CoA
-
a product analogue, protein-ligand interactions, complex structure, overview
1-hydroxy-2-naphthoyl-CoA
a product analogue, protein-ligand interactions, complex structure, overview
salicyloyl-CoA
-
protein-ligand interactions, complex structure, overview
salicyloyl-CoA
protein-ligand interactions, complex structure, overview
additional information
-
little or no inhibition by dimethylamide
-
additional information
2-amino-4-oxo-4-phenylbutanoate inhibitors are unstable in solution and eliminate to form the corresponding 4-oxo-4-phenylbut-2-enoates that then react with CoA in situ to form nanomolar inhibitors of MenB. The potency of these compounds results from interaction of the CoA adduct carboxylate with the MenB oxyanion hole, a conserved structural motif in the crotonase superfamily. No inhibition by 1548L21 at 0.3 mM
-
additional information
-
2-amino-4-oxo-4-phenylbutanoate inhibitors are unstable in solution and eliminate to form the corresponding 4-oxo-4-phenylbut-2-enoates that then react with CoA in situ to form nanomolar inhibitors of MenB. The potency of these compounds results from interaction of the CoA adduct carboxylate with the MenB oxyanion hole, a conserved structural motif in the crotonase superfamily. No inhibition by 1548L21 at 0.3 mM
-
additional information
-
little or no inhibition by dimethylamide
-
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0.000106
2-CoA-4-(2,4-dichlorophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.000135
2-CoA-4-(2-bromophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.000103
2-CoA-4-(2-chlorophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.000204
2-CoA-4-(2-fluorophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.000421
2-CoA-4-(2-iodophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0121
2-CoA-4-(2-methoxyphenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.000154
2-CoA-4-(2-nitrophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0141
2-CoA-4-(3-chlorophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.00047
2-CoA-4-(4-dichlorophenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0335
2-CoA-4-(4-methoxyphenyl)-4-oxobutanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.4
3-(2,4-dichlorophenyl)-3-oxopropyl-CoA
Mycobacterium tuberculosis
above, pH 7.4, 25°C
0.0022
4-(2,4-dichlorophenyl)-4-oxobutanoyl-CoA
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0084
4-(2-chlorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.12
4-(2-methoxyphenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
117
4-(4-chlorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0144
4-(4-fluorophenyl)-4-oxo-2-[[(1S)-1-phenylethyl]amino]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0032
4-oxo-2-[[(1S)-1-phenylethyl]amino]-4-[2-(trifluoromethyl)phenyl]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.0527
4-oxo-4-phenyl-2-[[(1S)-1-phenylethyl]amino]butanoic acid
Mycobacterium tuberculosis
pH 7.4, 25°C
0.01
methyl (2Z)-(2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
non-competitive inhibitor Ki' = 0.067 mM, pH not specified in the publication, temperature not specified in the publication
0.0241
methyl (2Z)-(5-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0463
methyl (2Z)-(6-chloro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
non-competitive inhibitor Ki' = 0.0185 mM, pH not specified in the publication, temperature not specified in the publication
0.027
methyl (2Z)-(6-fluoro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
non-competitive inhibitor Ki' = 0.0101 mM, pH not specified in the publication, temperature not specified in the publication
0.0231
methyl (2Z)-(6-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0282
methyl (2Z)-(6-nitro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0357
methyl (2Z)-(7-chloro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.03
methyl (2Z)-(7-fluoro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0182
methyl (2Z)-(7-methyl-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0203
methyl (2Z)-(7-nitro-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene)ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0179
methyl (2Z)-[6-(ethylsulfonyl)-2-oxo-2H-1,4-benzoxazin-3(4H)-ylidene]ethanoate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
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metabolism
-
the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2
metabolism
the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2
metabolism
-
the enzyme is involved in the menaquinone biosynthesis
metabolism
the enzyme is involved in the menaquinone biosynthesis
physiological function
-
the enzyme is an essential enzyme in vitamin K biosynthesis
physiological function
the enzyme is an essential enzyme in vitamin K biosynthesis
additional information
active site structure, catalytically essential is Asp185 in the active site, residues Gly77 and Gly123 form an oxyanion hole for stabilization of the enolate intermediate, a hydrophobic patch consisting of Leu96, Val98, and Leu99 for recognition and interaction with the nonpolar aromatic ring of the substrate, and other catalytically essential motifs consisting of Ser151, Asp153, and Tyr248 from a different subunit, detailed overview and modeling
additional information
-
active site structure, catalytically essential is Gly156 in the active site, residues Gly86 and Gly133 form an oxyanion hole for stabilization of the enolate intermediate, a hydrophobic patch consisting of Leu106, Val108, and Leu109 for recognition and interaction with the nonpolar aromatic ring of the substrate, and other catalytically essential motifs consisting of Ser161, Asp163, and Tyr258 from a different subunit, detailed overview and modeling
additional information
enzyme structure in complex with a product analogue, the structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. A new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand
additional information
-
enzyme structure in complex with a product analogue, the structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. A new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand
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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
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Meganathan, R.; Bentley, R.
Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes
J. Bacteriol.
140
92-98
1979
Mycolicibacterium phlei
brenda
Kolkmann, R.; Leistner, E.
4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis
Z. Naturforsch. C
42
1207-1214
1987
Escherichia coli, Galium mollugo, Mycolicibacterium phlei
brenda
Heide, L.; Leistner, E.
Enzymatic synthesis of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis
FEBS Lett.
128
201-204
1981
Mycolicibacterium phlei
brenda
Shaw, D.J.; Robinson, E.C.; Meganathan, R.; Bentley, R.; Guest, J.R.
Recombinent plasmids containing menaquinone biosynthetic genes of Escherichia coli
FEMS Microbiol. Lett.
17
63-67
1983
Escherichia coli
-
brenda
Heide, L.; Arendt, S.; Leistner, E.
Enzymatic synthesis, characterization, and metabolism of the coenzyme A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis
J. Biol. Chem.
257
7396-7400
1982
Escherichia coli, Mycolicibacterium phlei
brenda
Johnston, J.M.; Arcus, V.L.; Baker, E.N.
Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms
Acta Crystallogr. Sect. D
61
1199-1206
2005
Mycobacterium tuberculosis (P9WNP5), Mycobacterium tuberculosis
brenda
Kanaujia, S.P.; Ranjani, C.V.; Jeyakanthan, J.; Baba, S.; Kuroishi, C.; Ebihara, A.; Shinkai, A.; Kuramitsu, S.; Shiro, Y.; Sekar, K.; Yokoyama, S.
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of DHNA synthetase from Geobacillus kaustophilus
Acta Crystallogr. Sect. F
63
103-105
2007
Geobacillus kaustophilus
brenda
Ulaganathan, V.; Agacan, M.F.; Buetow, L.; Tulloch, L.B.; Hunter, W.N.
Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA
Acta Crystallogr. Sect. F
63
908-913
2007
Staphylococcus aureus (Q5HH38), Staphylococcus aureus
brenda
Lannergard, J.; von Eiff, C.; Sander, G.; Cordes, T.; Seggewiss, J.; Peters, G.; Proctor, R.A.; Becker, K.; Hughes, D.
Identification of the genetic basis for clinical menadione-auxotrophic small-colony variant isolates of Staphylococcus aureus
Antimicrob. Agents Chemother.
52
4017-4022
2008
Staphylococcus aureus
brenda
Babujee, L.; Wurtz, V.; Ma, C.; Lueder, F.; Soni, P.; van Dorsselaer, A.; Reumann, S.
The proteome map of spinach leaf peroxisomes indicates partial compartmentalization of phylloquinone (vitamin K1) biosynthesis in plant peroxisomes
J. Exp. Bot.
61
1441-1453
2010
Spinacia oleracea
brenda
Chen, M.; Jiang, M.; Sun, Y.; Guo, Z.; Guo, Z.
Stabilization of the second oxyanion intermediate by 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase of the menaquinone pathway: Spectroscopic evidence of the involvement of a conserved aspartic acid
Biochemistry
50
5893-5904
2011
Escherichia coli
brenda
Li, H.J.; Li, X.; Liu, N.; Zhang, H.; Truglio, J.J.; Mishra, S.; Kisker, C.F.; Garcia-Diaz, M.; Tonge, P.J.
Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member
Biochemistry
50
9532-9544
2011
Escherichia coli, Mycobacterium tuberculosis (P9WNP5), Mycobacterium tuberculosis
brenda
Li, X.; Liu, N.; Zhang, H.; Knudson, S.E.; Slayden, R.A.; Tonge, P.J.
Synthesis and SAR studies of 1,4-benzoxazine MenB inhibitors: novel antibacterial agents against Mycobacterium tuberculosis
Bioorg. Med. Chem. Lett.
20
6306-6309
2010
Mycobacterium tuberculosis
brenda
Li, X.; Liu, N.; Zhang, H.; Knudson, S.E.; Li, H.J.; Lai, C.T.; Simmerling, C.; Slayden, R.A.; Tonge, P.J.
CoA adducts of 4-oxo-4-phenylbut-2-enoates: inhibitors of MenB from the M. tuberculosis menaquinone biosynthesis pathway
ACS Med. Chem. Lett.
2
818-823
2011
Mycobacterium tuberculosis (P9WNP5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNP5)
brenda
Sun, Y.; Song, H.; Li, J.; Jiang, M.; Li, Y.; Zhou, J.; Guo, Z.
Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme a synthases from vitamin K biosynthetic pathways
Biochemistry
51
4580-4589
2012
Escherichia coli, Synechocystis sp. (P73495)
brenda
Sun, Y.; Song, H.; Li, J.; Li, Y.; Jiang, M.; Zhou, J.; Guo, Z.
Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme A synthase from the crotonase fold superfamily
PLoS ONE
8
e63095
2013
Escherichia coli, Synechocystis sp. (P73495), Synechocystis sp.
brenda
Song, H.; Sung, H.P.; Tse, Y.S.; Jiang, M.; Guo, Z.
Ligand-dependent active-site closure revealed in the crystal structure of Mycobacterium tuberculosis MenB complexed with product analogues
Acta Crystallogr. Sect. D
70
2959-2969
2014
Mycobacterium tuberculosis (P9WNP5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNP5)
brenda
Passi, A.; Rajput, N.K.; Wild, D.J.; Bhardwaj, A.
RepTB a gene ontology based drug repurposing approach for tuberculosis
J. Cheminform.
10
24
2018
Mycobacterium tuberculosis
brenda