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discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: O-succinylbenzoate-CoA ligase

Species: Galium mollugo

Summary:
Protein extracts obtained from cell cultures of Galium mollugo mediate the conversion of 2-succinylbenzoate (OSB) to 4-(2'-carboxyphenyl)-4-oxobutyryl-CoA in the presence of CoA and ATP [Heide82a]. Three CoA esters are generated under in vitro conditions, the mono-CoA ester 4-(2'-carboxyphenyl)-4-oxobutyryl CoA ("aliphatic" CoA, described in this pathway), the mono-CoA ester 2-(3'-carboxypropionyl)benzoyl CoA ("aromatic" CoA), and a di-CoA ester, 4-(2'-carboxyphenyl)-4-oxobutyryl-di-CoA. However, only the "aliphatic" CoA ester was further convertable to 1,4-dihydroxy-2-naphtoic acid (DHNA) by a microbial naphtoate synthase enzyme, indicating that this isomer is the true in vivo product [Kolkmann87].

Unlike the bacterial O-succinylbenzoate-CoA ligase which is AMP and diphosphate forming, the plant enzyme is activated by ATP with ADP and phosphate forming. ADP and phosphate have product inhibition of the enzyme activity. A 50% inhibition was observed with 5.3 mM ADP, and 0.35 mM phosphate, respectively. The enzyme is highly substrate specific. Analogues of O-succinoylbenzoate such as O-malonylbenzoate, benzoylpropionate, benzoate, 2-acetylbenzoate and p-coumarate were not accepted. The enzyme activity requires Mg2+. Ca2+, Cu2+ and Zn2+ could not replace Mg2+, whereas, Ni2+ (85% compared to Mg2+), Mn2+ (75%) and Co2+ (66%) gave partial activity [Sieweke92].

Gene-Reaction Schematic: ?

Credits:
Revised 08-Feb-2008 by Zhang P


Enzymatic reaction of: O-succinylbenzoate-CoA ligase

ATP + 2-succinylbenzoate + coenzyme A <=> 4-(2'-carboxyphenyl)-4-oxobutyryl-CoA + ADP + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of phylloquinol biosynthesis , 1,4-dihydroxy-2-naphthoate biosynthesis II (plants)

Cofactors or Prosthetic Groups: Mg2+ [Sieweke92, Kolkmann87]

T(opt): 28 °C [Sieweke92]

pH(opt): 6.8 [Sieweke92]


References

Heide82a: Heide L, Kolkmann R, Arendt S, Leistner E (1982). "Enzymic synthesis of o-succinylbenzoyl-CoA in cell-free extracts of anthraquinone producing Galium mollugo L. cell suspension cultures." Plant Cell Reports, 1, 180-182.

Kolkmann87: Kolkmann R, Leistner E (1987). "4-2'-(carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K (menaquinone) biosynthesis." Z. Naturforsch., 42c, 1207-1214.

Sieweke92: Sieweke, Hans-Jurgen, Leistner, Eckhard (1992). "O-succinylbenzoate: coenzyme A ligase from anthraquinone producing cell suspension cultures of Galium mollugo." Phytochemistry 31(7): 2329-2335.


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13B.