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Literature summary extracted from

  • Odokonyero, D.; McMillan, A.W.; Ramagopal, U.A.; Toro, R.; Truong, D.P.; Zhu, M.; Lopez, M.S.; Somiari, B.; Herman, M.; Aziz, A.; Bonanno, J.B.; Hull, K.G.; Burley, S.K.; Romo, D.; Almo, S.C.; Glasner, M.E.
    Comparison of Alicyclobacillus acidocaldarius o-succinylbenzoate synthase to its promiscuous N-succinylamino acid racemase/o-succinylbenzoate synthase relatives (2018), Biochemistry, 57, 3676-3689 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.113 Y299I naturally occuring mutation, identified by molecular modeling and sequence conservation within the NSAR/OSBS subfamily, the mutation increases NSAR activity from without affecting OSBS activity. The mutation does not appear to affect binding affinity but instead affects kcat, by reorienting the substrate or modifying conformational changes to allow both catalytic lysines to access the proton that is moved during the reaction Alicyclobacillus acidocaldarius subsp. acidocaldarius
4.2.1.113 Y299I/M18F site-directed mutagenesis, while the Y299I mutation increases NSAR activity, the second mutation M18F obliterates this gain of activity, epistatic interference by M18F Alicyclobacillus acidocaldarius subsp. acidocaldarius

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.113 N-succinylphenylglycine competitive inhibition, molecular modeling showing that AaOSBS binds N-succinylphenylglycine with moderate affinity in a site that overlaps its normal substrate Alicyclobacillus acidocaldarius subsp. acidocaldarius

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.113 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Alicyclobacillus acidocaldarius subsp. acidocaldarius
-
 2-succinylbenzoate + H2O
-
 ?
4.2.1.113 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A
-
 2-succinylbenzoate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.113 Alicyclobacillus acidocaldarius subsp. acidocaldarius C8WS29 i.e. Bacillus acidocaldarius
-
4.2.1.113 Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A C8WS29 i.e. Bacillus acidocaldarius
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.113 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius 2-succinylbenzoate + H2O
-
 ?
4.2.1.113 (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A 2-succinylbenzoate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.113 AaOSBS
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
4.2.1.113 menC
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
4.2.1.113 OSBS
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius

General Information

EC Number General Information Comment Organism
4.2.1.113 evolution the evolution of catalytically promiscuous enzymes like those from the N-succinylamino acid racemase/o-succinylbenzoate synthase (NSAR/OSBS) subfamily can reveal mechanisms by which new functions evolve. Additional sites influence the evolution of NSAR reaction specificity in the NSAR/OSBS subfamily Alicyclobacillus acidocaldarius subsp. acidocaldarius
4.2.1.113 additional information competitive inhibition and molecular modeling show that AaOSBS binds N-succinylphenylglycine with moderate affinity in a site that overlaps its normal substrate Alicyclobacillus acidocaldarius subsp. acidocaldarius