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4.1.1.85: 3-dehydro-L-gulonate-6-phosphate decarboxylase

This is an abbreviated version!
For detailed information about 3-dehydro-L-gulonate-6-phosphate decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.85

Reaction

3-dehydro-L-gulonate 6-phosphate
+
H+
=
L-xylulose 5-phosphate
 +
CO2

Synonyms

3-keto-L-gulonate 6-phosphate decarboxylase, KGPDC, More, SgaH, SgbH, UlaD

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.85 3-dehydro-L-gulonate-6-phosphate decarboxylase

Engineering

Engineering on EC 4.1.1.85 - 3-dehydro-L-gulonate-6-phosphate decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E112Q
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
E112Q/H136A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
H136A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
K64A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
D67A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D67A/H136A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
D67N
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D67N/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112A/H136A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112A/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112D/R139V
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112D/R139V/T169A
E112D/R139V/T169A/R192A
-
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112D/T169A
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112Q/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112Q/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E33K
-
site-directed mutagenesis, inactive mutant
H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136A/R139V
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136N
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/E112A/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
K64A/E112Q/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/R139V
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64R
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K64R/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R139V
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme