Cloned (Comment) | Organism |
---|---|
recombinant expression | Escherichia coli |
recombinant expression | Synechocystis sp. |
Crystallization (Comment) | Organism |
---|---|
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 | Escherichia coli |
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 | Synechocystis sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
bicarbonate | the enzyme from Escherichia coli is a type I enzyme, which is dependent on exogenous bicarbonate for catalytic activity. The bicarbonate cofactor is bound to the enzyme active site at a position equivalent to that of the side chain carboxylate of an aspartate residue conserved among bicarbonate-insensitive DHNA-CoA synthases, binding site structure, overview | Escherichia coli | |
bicarbonate | the enzyme from Synechocystis is a type I enzyme, type I enzymes are dependent on exogenous bicarbonate for catalytic activity. The bicarbonate cofactor is bound to the enzyme active site at a position equivalent to that of the side chain carboxylate of an aspartate residue conserved among bicarbonate-insensitive DHNA-CoA synthases, binding site structure, overview | Synechocystis sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
o-succinylbenzoate + CoA | Escherichia coli | - |
1,4-dihydroxy-2-naphthoyl-CoA + H2O | - |
? | |
o-succinylbenzoate + CoA | Synechocystis sp. | - |
1,4-dihydroxy-2-naphthoyl-CoA + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synechocystis sp. | P73495 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Escherichia coli |
recombinant enzyme | Synechocystis sp. |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O | the enzyme is an essential enzyme in vitamin K biosynthesis, which is responsible for conversion of o-succinylbenzoyl-CoA to 1,4-dihydroxy-2-naphthoyl-CoA via catalysis of a multiple-step intramolecular Claisen condensation reaction, proposed reaction mechanism, overview | Synechocystis sp. | |
4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O | the enzyme is an essential enzyme in vitamin K biosynthesis, which is responsible for conversion of o-succinylbenzoyl-CoA to DHNACoA via catalysis of a multiple-step intramolecular Claisen condensation reaction, proposed reaction mechanism, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
o-succinylbenzoate + CoA | - |
Escherichia coli | 1,4-dihydroxy-2-naphthoyl-CoA + H2O | - |
? | |
o-succinylbenzoate + CoA | - |
Synechocystis sp. | 1,4-dihydroxy-2-naphthoyl-CoA + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
1,4-dihydroxy-2-naphthoyl coenzyme A synthase | - |
Escherichia coli |
1,4-dihydroxy-2-naphthoyl coenzyme A synthase | - |
Synechocystis sp. |
DHNA-CoA synthase | - |
Escherichia coli |
DHNA-CoA synthase | - |
Synechocystis sp. |
MenB | - |
Escherichia coli |
MenB | - |
Synechocystis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Escherichia coli |
7 | - |
assay at | Synechocystis sp. |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2 | Escherichia coli |
metabolism | the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2 | Synechocystis sp. |
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 | Synechocystis sp. |
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 | Escherichia coli |
physiological function | the enzyme is an essential enzyme in vitamin K biosynthesis | Escherichia coli |
physiological function | the enzyme is an essential enzyme in vitamin K biosynthesis | Synechocystis sp. |