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Literature summary for 4.2.1.113 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
Search for more literature for 4.2.1.113

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Alicyclobacillus acidocaldarius subsp. acidocaldarius
-
 2-succinylbenzoate + H2O
-
 ?
(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

Organism UniProt Comment Textmining
Alicyclobacillus acidocaldarius subsp. acidocaldarius C8WS29 i.e. Bacillus acidocaldarius
-
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius 2-succinylbenzoate + H2O
-
 ?
(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

Synonyms Comment Organism
AaOSBS
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
menC
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius
OSBS
-
 Alicyclobacillus acidocaldarius subsp. acidocaldarius

General Information

General Information Comment Organism
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
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