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6.2.1.26: O-succinylbenzoate-CoA ligase

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

Word Map on EC 6.2.1.26

Reaction

ATP
+
2-succinylbenzoate
 +
CoA
=
AMP
 +
diphosphate
 +
4-(2-carboxyphenyl)-4-oxobutanoyl-CoA

Synonyms

AAE14, acyl-activating enzyme 14, BsMenE, MenE, O-succinylbenzoate-CoA synthase, o-succinylbenzoate-CoA synthetase, o-succinylbenzoyl-CoA synthetase, o-succinylbenzoyl-coenzyme A ligase, o-succinylbenzoyl-coenzyme A synthetase, OSB-CoA ligase, OSB-CoA synthetase, OSB:CoA ligase, synthetase, o-succinylbenzoyl coenzyme A

ECTree

     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.26 O-succinylbenzoate-CoA ligase

Engineering

Engineering on EC 6.2.1.26 - O-succinylbenzoate-CoA ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G154P
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
G157P
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
R382A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
R382K
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T152A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T155A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T155A/T156A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
T156A
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
R382A
-
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
-
T152A
-
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
-
T155A
-
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
-
T156A
-
site-directed mutagenesis, the mutant shows the same stability and circular dichroism spectra as the wild-type enzyme, but reduced catalytic activity
-
H341A
-
mutant enzyme loses 65% of ist activity and the Km-value for ATP increases 5.4fold
additional information