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
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4.1.1.47
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glycerate
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photorespiration
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alpha-ketoglutarate
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hydroxypyruvate
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hyperoxaluria
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photorespiratory
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acetohydroxy
- 4.1.1.47
- glycerate
-
photorespiration
- alpha-ketoglutarate
- hydroxypyruvate
- hyperoxaluria
-
photorespiratory
-
acetohydroxy
Reaction
2 glyoxylate
=
Synonyms
GCL, Glyoxalate carboligase, Glyoxylate carbo-ligase, Glyoxylate carboligase, Glyoxylate carboxy-lyase, Glyoxylate carboxy-lyase (dimerizing and reducing), Glyoxylic carbo-ligase, Hydroxymalonic semialdehyde carboxylase, Synthase, tartronate semialdehyde, Tartronate semialdehyde carboxylase, tartronate semialdehyde synthase, Tartronate-semialdehyde synthase, Tartronic semialdehyde carboxylase, Tartronic semialdehyde synthase
ECTree
4.1.1.47 tartronate-semialdehyde synthaseAdvanced search results
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Engineering on EC 4.1.1.47 - tartronate-semialdehyde synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
I393A
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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
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the mutation leads to a lower catalytic efficiency (5.3%) compared to the wild type enzyme
I479V
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the mutation leads to a lower catalytic efficiency (4.8%) compared to the wild type enzyme
L478A
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the mutation leads to a lower catalytic efficiency (0.34%) compared to the wild type enzyme
V51D
V51D/I393A
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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
V51E
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the mutant is less active than the wild type enzyme (turnover rates are 7fold lower) despite having higher rate of activation of the coenzyme
V51D
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replacement of Val51 by an amino acid with a carboxylate in its side chain (glutamate or aspartate) has striking and significant effects, V51D variant of glyoxylate carboligase undergoes proton exchange at a rate 6fold higher than the wild-type enzyme
V51D
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the substitution shifts the pH optimum to 6.0-6.2, the mutant is less active (1.2%) than the wild type enzyme (turnover rates are 2 orders of magnitude lower) despite having higher rate of activation of the coenzyme
