O-succinylbenzoate—CoA ligase
| o-Succinylbenzoate—CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
o-Succinylbenzoate—CoA ligase (
Background
The systematic name for the MenE enzyme is 2-succinylbenzoate: CoA ligase (AMP-forming). Other names for this enzyme include: o-succinylbenzoate-CoA synthase; o-succinylbenzoyl-coenzyme A synthetase; OSB-CoA synthetase; OSB: CoA ligase; synthetase, and o-succinylbenzoyle coenzyme A. The EC number is 6.2.1.26. MenE belongs to the ligase enzyme family, or class 6.
In the presence of 0.5mM of Ca(2+), K(+), Na(+), and Zn(2+) the enzyme activity was increased twofold. In the presence of .5 mM of Co(2+) and Mn(2+) the enzyme activity was increased fourfold. Mg(2+) is the ion that increases the enzyme activity the most. With .5 mM of Mg(2+) enzyme activity was increased sixfold. Inhibitors of this enzyme include diethylprocarbonate, Fe(2+), Hg(2+), and Mg(2+) (above 1mM).[2]
The maximum specific enzymatic activity is 3.2 micromol/min/mg. The optimum pH is 7.5. The maximum pH is 8. The optimum temperature is 30 degrees Celsius and the maximum temperature is 40 degrees Celsius. The molecular weight of o-succinylbenzoate CoA ligase is 185000 Da or 185 kDa. This enzyme is a tetramer, meaning it has four subunits in its quaternary structure.[2]
The PDB accession code is 3ipl. This is the crystal structure for o-succinylbenzoate CoA ligase in
Pathway
The pathway o-succinylbenzoate CoA ligase belongs to is called 1, 4-dihydroxy-2-napthoate biosynthesis I. Other organisms that contain this pathway are eukaryotic bacteria such as Bacillus anthracis.[4] Organisms that contain a pathway similar to this include Arabidopsis thaliana (gene AAE14),[5] Mycobacterium phlei,[6] and Synechocystis sp. (gene PCC 6803).[7] The reason for the difference in pathways is due to the varying functions of Vitamin K. Eukaryotic bacteria use vitamin K II while other organisms use vitamin K I. Other pathways that include o-succinylbenzoate CoA ligase include 1, 4-diydroxy-2-naphthoate biosynthesis II (i.e. in Arabidopsis thaliana), biosynthesis of secondary metabolites, metabolic pathways, ubiquinone, and other terpenoid-quinone biosynthesis. In Bacillus anthracis this enzyme is a target of potential antibiotic discovery.
Reaction
The reaction in vitamin K synthesis that includes MenE is as follows:
ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
The substrates of this reaction are
References
- ^ van Oostende, Widhalm, Furt, Ducluzeau, Basset (2011). Phylloquinone (Vitamin K1): function, enzymes and genes. Advances in Botanical Research: Academic Press (Amsterdam). pp. 229–61.
{{cite book}}: CS1 maint: multiple names: authors list (link) - ^ PMID 8955296.
- ^ Patskovsky, Toro, Dickey, Sauder, Chang, Burley, Almo. "Crystal structure of o-succinylbenzoic acid-CoA ligase from Staphylococcus aureus". PDB. RCSB. Retrieved 6 December 2014.
{{cite web}}: CS1 maint: multiple names: authors list (link) - PMID 18973344.
- PMID 18208520.
- S2CID 12789671.
- PMID 12615349.)
{{cite journal}}: CS1 maint: multiple names: authors list (link - S2CID 41701934.
