O-succinylbenzoate—CoA ligase: Difference between revisions
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Revision as of 11:00, 7 February 2015
 | This article needs more links to other articles to help integrate it into the encyclopedia. (December 2014) |
O-succinylbenzoate CoA ligase (6.2.1.26), encoded from the menE gene in Escherichia coli, catalyzes the fifth reaction in the synthesis of menaquinone (vitamin K2). This pathway is called 1, 4-dihydroxy-2-naphthoate biosynthesis I.[1] Vitamin K is a quinone that serves as an electron transporter during anaerobic respiration. This process of anaerobic respiration allows the bacteria to generate the energy required to survive.
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|---|---|
| Identifiers | |
| EC Number | 6.2.1.26 |
| Databases | |
| BRENDA | BRENDA entry |
| ExplorEnz | ExplorEnz entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PubMed | articles |
| IUBMB | enzyme nomenclature |
| PROSITE | PROSITE documentation |
| SYSTERS | enzyme families |
| InterPro | InterPro entry |
| PDB | PDB structure |
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 .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.[3]
The PDB accession code is 3ipl. This is the crystal structure for o-succinylbenzoate CoA ligase in Staphylococcus aureus (strain N315) because the structure for E. coli has not been crystalized as of yet.[4]
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.[5] Organisms that contain a pathway similar to this include Arabidopsis thaliana (gene AAE14),[6] Mycobacterium phlei,[7] and Synechocystis sp. (gene PCC 6803).[8] 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 ATP, CoA, and 2-succinylbenzoate. The cofactors are ATP and CoA. The products are AMP, diphosphate, and 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA.[9]
Resources
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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) - ^ Kwon, Bhattacharyya, Meganathan (December 1996). "Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli". PubMed. PMID 8955296. Retrieved 6 December 2014.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kwon, Bhattacharyya, Meganathan (December 1996). "Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli". PubMed. PMID 8955296. Retrieved 6 December 2014.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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) - ^ Tian, Suk, Cai, Crich, Mesecar (25 November 2008). "Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate". PubMed. PMID 18973344. Retrieved 6 December 2014.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kim, van Oostende, Basset, Browse (April 2008). "The AAE14 gene encodes the Arabidopsis o-succinylbenzoyl-CoA ligase that is essential for phylloquinone synthesis and photosystem-I function". PubMed. PMID 18208520. Retrieved 6 December 2014.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Sieweke, Leistner (August 1991). "o-Succinylbenzoate: coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis, displays broad specificity". PubMed. PMID 1663748. Retrieved 6 December 2014.
- ^ Johnson, Naithani, Stewart Jr., Zybailov, Jones, Golbeck, Chitnis (6 March 2003). "The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803". Biochimica et Biophysica Acta (BBA)- Bioenergetics. doi:10.1016/S0005-2728(02)00396-1. Retrieved 6 December 2014.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kolkmann, Leistner (December 1987). "4-(2'-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis". PubMed. PMID 2966501. Retrieved 6 December 2014.