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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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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 Sat Dec 20, 2014, biocyc13.