4.1.1.47: tartronate-semialdehyde synthase

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

Word Map on EC 4.1.1.47

Reaction

2 glyoxylate =

2-hydroxy-3-oxopropanoate
+
CO2

Synonyms

Synthase, tartronate semialdehyde, Tartronate semialdehyde carboxylase, Glyoxylate carbo-ligase, Glyoxylic carbo-ligase, Hydroxymalonic semialdehyde carboxylase, Tartronic semialdehyde synthase, Tartronic semialdehyde carboxylase, Glyoxalate carboligase, Glyoxylate carboligase, Glyoxylate carboxy-lyase, Glyoxylate carboxy-lyase (dimerizing and reducing), Tartronate-semialdehyde synthase, GCL, tartronate semialdehyde synthase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.47 tartronate-semialdehyde synthase

Engineering

Engineering on EC 4.1.1.47 - tartronate-semialdehyde synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V51E
-
the mutant is less active than the wild type enzyme (turnover rates are 7fold lower) despite having higher rate of activation of the coenzyme
L478A
-
the mutation leads to a lower catalytic efficiency (0.34%) compared to the wild type enzyme
I393A
-
the mutation leads to a lower catalytic efficiency (3.9%) compared to the wild type enzyme. The enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme
I393V
-
the mutation leads to a lower catalytic efficiency (5.3%) compared to the wild type enzyme
I479V
-
the mutation leads to a lower catalytic efficiency (4.8%) compared to the wild type enzyme
V51D/I393A
-
the enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme
E52Q
site-directed mutagenesis
V51E
site-directed mutagenesis
V51D
site-directed mutagenesis
V51S
site-directed mutagenesis