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