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4.2.1.113: o-succinylbenzoate synthase

This is an abbreviated version!
For detailed information about o-succinylbenzoate synthase, go to the full flat file.

Word Map on EC 4.2.1.113

Reaction

(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
=
2-succinylbenzoate
 +
H2O

Synonyms

AaOSBS, ExiOSBS, menC, Mtb-OSBS, o-succinylbenzoate synthase, o-succinylbenzoic acid synthase, OSB synthase, OSBS

ECTree

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.113 o-succinylbenzoate synthase

Engineering

Engineering on EC 4.2.1.113 - o-succinylbenzoate synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
Y299I
Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A
-
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
-
Y299I/M18F
Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A
-
site-directed mutagenesis, while the Y299I mutation increases NSAR activity, the second mutation M18F obliterates this gain of activity, epistatic interference by M18F
-
K163R
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(S)-phenylglycine with solvent hydrogen
K163S
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(S)-phenylglycine with solvent hydrogen
K263R
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(R)-phenylglycine with solvent hydrogen
K263S
-
no o-succinylbenzoate synthase activity and no N-acylamino acid racemase activity, mutant enzyme catalyzes the stereospecific exchange of the alpha-hydrogen of N-succinyl-(R)-phenylglycine with solvent hydrogen
F51A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G16P/V17F/V18R/L19T/R20S/D21F/R22G/R23T/L24QL48A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G288A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, G288A introduces a steric clash with the substrate, reducing kcat/KM over 500fold
G295A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
I265A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K133A
inactive mutant
K133R
inactive mutant
K133S
inactive mutant
K235A
inactive mutant
K235R
inactive mutant
K235S
inactive mutant
L109A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L19A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48A/F51A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L48M/F51Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R159M
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S262A/S263A/S264A/I265A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S262T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S263G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S264A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T291S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V233N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F16A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
F39A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
G254A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
G254T
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73A/T75A
site-directed mutagenesis, the mutant is inactive
N73A/T75L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
N73L/T75V
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R128M
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R15G/F16G/R17G/G18G/I19G
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A/F39A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
R17A/Y42A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
T75A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
T75L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
V230L
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
Y42A
site-directed mutagenesis, the mutant enzyme activity is reduced compared to the wild-type enzyme
additional information
-
20s loop is truncated by deleting residues V17, V18, L19, R20, D21, R22, R23, and L24 resulting in a mutant with highly reduced activity compared to the wild-type enzyme