MetaCyc Enzyme: O-succinylbenzoate-CoA ligase

Species: Galium mollugo

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 [Heide82].

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].

Note that the authors have reported production of ADP, which is unlike the bacterial O-succinylbenzoate-CoA ligase, which forms AMP. However, while ADP was formed in large quantities, some AMP was formed as well, and thus the authors did not rule out that formation of AMP could also be catalysed by the ligase, which may be non-specific with respect to ATP hydrolysis.

The enzyme is highly substrate specific. Analogues of O-succinoylbenzoate such as O-malonylbenzoate, benzoylpropionate, benzoate, 2-acetylbenzoate and p-coumarate were not accepted.

Activity requires Mg2+. While Ca2+, Cu2+ and Zn2+ could not replace Mg2+, Ni2+ (85% compared to Mg2+), Mn2+ (75%) and Co2+ (66%) gave partial activity [Sieweke92].

Gene-Reaction Schematic

Gene-Reaction Schematic

Revised 08-Feb-2008 by Zhang P

Enzymatic reaction of: O-succinylbenzoate-CoA ligase

Inferred from experiment

EC Number:

2-succinylbenzoate + ATP + coenzyme A → 4-(2'-carboxyphenyl)-4-oxobutyryl-CoA + AMP + diphosphate

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of phylloquinol biosynthesis, 1,4-dihydroxy-2-naphthoate biosynthesis

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

T(opt): 28 °C [Sieweke92]

pH(opt): 6.8 [Sieweke92]


Heide82: 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.

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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