EC 4.2.1.113 - o-succinylbenzoate synthase

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IntEnz Enzyme Nomenclature
EC 4.2.1.113

Names

Accepted name:
o-succinylbenzoate synthase
Other names:
o-succinylbenzoic acid synthase
OSB synthase
OSBS
2-succinylbenzoate synthase
menC
Systematic name:
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate hydrolyase (2-succinylbenzoate-forming)

Reaction

Cofactor

Comments:

Belongs to the enolase superfamily and requires divalent cations, preferably Mg2+ or Mn2+, for activity. Forms part of the vitamin-K-biosynthesis pathway.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
CAS Registry Number: 97089-83-3
UniProtKB/Swiss-Prot: (81) [show] [UniProt]

References

  1. Sharma, V., Meganathan, R. and Hudspeth, M.E.S.
    Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and expression of the menC gene from Escherichia coli.
    J. Bacteriol. 175: 4917-4921 (1993). [PMID: 8335646]
  2. Klenchin, V.A., Taylor Ringia, E.A., Gerlt, J.A. and Rayment, I.
    Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli.
    Biochemistry 42: 14427-14433 (2003). [PMID: 14661953]
  3. Palmer, D.R., Garrett, J.B., Sharma, V., Meganathan, R., Babbitt, P.C. and Gerlt, J.A.
    Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase.
    Biochemistry 38: 4252-4258 (1999). [PMID: 10194342]
  4. Thompson, T.B., Garrett, J.B., Taylor, E.A., Meganathan, R., Gerlt, J.A. and Rayment, I.
    Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate.
    Biochemistry 39: 10662-10676 (2000). [PMID: 10978150]
  5. Taylor Ringia, E.A., Garrett, J.B., Thoden, J.B., Holden, H.M., Rayment, I. and Gerlt, J.A.
    Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis.
    Biochemistry 43: 224-229 (2004). [PMID: 14705949]

[EC 4.2.1.113 created 2007]