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4.1.1.31: phosphoenolpyruvate carboxylase

This is an abbreviated version!
For detailed information about phosphoenolpyruvate carboxylase, go to the full flat file.

Word Map on EC 4.1.1.31

Reaction

phosphate
+
oxaloacetate
=
phosphoenolpyruvate
 +
HCO3-

Synonyms

archaeal-type phosphoenolpyruvate carboxylase, AT1G53310, atPEPC, Atppc1, Atppc2, Atppc3, Atppc4, bacterial-type PEPC, bacterial-type phosphoenolpyruvate carboxylase, BPTC, BTPC, C4 PEPC, C4-PEPC, Carboxylase, phosphopyruvate (phosphate), Class-1 PEPC, Class-2 PEPC, CP21, CP28, CP46, CrPpc1, CrPpc2, Hvpepc3, Hvpepc4, Hvpepc5, Ljpepc1, NCgl1523, OJ1484_G09.129-1, Osppc2a, Osppc4, PEOC, PEP carboxylase, PEP-carboxylase, PEPC, PEPC(p102)kinase, PEPC1, PEPC2, PEPC3, PEPC7, PepcA, PEPCase, PEPCase1, PEPCK, PEPK, phosphoenol pyruvate carboxylase, phosphoenolpyruvate carboxykinase, Phosphoenolpyruvate carboxylase, Phosphoenolpyruvic carboxylase, photosynthetic phosphoenolpyruvate carboxylase, plant-type phosphoenolpyruvate carboxylase, PPC, PPC1, PPC2, PPC2a, PPC3, PPC4, PpcA, PpcA1, PPCK1, PPCK2, PTPC, S.minutum PEPC1, Sb02g021090, Sb04g008720, SORBI_3007G106500, SSO2256, SvPEPC

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.31 phosphoenolpyruvate carboxylase

Engineering

Engineering on EC 4.1.1.31 - phosphoenolpyruvate carboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K112E
mutation at succinylation site, does not affect glutamate production
K112R
mutation at succinylation site, does not affect glutamate production
K653G
-
the mutation dramatically reduces the enzyme activity
K653Q
acetylation mimic mutation, abolishes glutamate production. Growth is not affected
K653R
non-acylation mimic mutant, retains glutamate production, the final glutamate concentration does not reach wild-type levels. Growth is not affected
K813G
-
the mutation does not significantly alter the enzyme activity
N917G
-
the mutation does not significantly alter the enzyme activity and results in about 37% improved L-lysine production
R620G
-
the mutation dramatically reduces the enzyme activity
R873G
-
the mutation does not significantly alter the enzyme activity
S869G
-
the mutation does not significantly alter the enzyme activity
K112E
-
mutation at succinylation site, does not affect glutamate production
-
K112R
-
mutation at succinylation site, does not affect glutamate production
-
K653Q
-
acetylation mimic mutation, abolishes glutamate production. Growth is not affected
-
K653R
-
non-acylation mimic mutant, retains glutamate production, the final glutamate concentration does not reach wild-type levels. Growth is not affected
-
K653G
-
the mutation dramatically reduces the enzyme activity
-
N917G
-
the mutation does not significantly alter the enzyme activity and results in about 37% improved L-lysine production
-
R620G
-
the mutation dramatically reduces the enzyme activity
-
R873G
-
the mutation does not significantly alter the enzyme activity
-
S869G
-
the mutation does not significantly alter the enzyme activity
-
R438C
Arg438Cys has an increased tendency to dissociate into dimers. Mutant enzyme Arg703Gly shows a 5fold decreased turnover number compared to the wild type enzyme
R703G/R703G
mutant enzyme Arg703Gly/Arg704Gly shows a 20fold decreased turnover number compared to the wild type enzyme
R884E
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
R884Q
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
R884S
the mutant is clearly less sensitive towards malate compared to the wild type enzyme
E946K
mutation renders the enzyme sensitive to inhibition by malate, aspartate, and fumarate
S12D
mutation of phosphorylatable serine
S425A
-
the mutant shows strongly increased Km values compared to the wild type enzyme
S425A/S451D
-
the mutant shows strongly increased Km values compared to the wild type enzyme
S451D
-
the mutant shows strongly increased Km values compared to the wild type enzyme
delataC1
deletion of the last c-terminal amino acid. kcat: 9.5/sec (phosphoenolpyruvate),12.6% of wild type catalytic activity
delataC4
deletion of the last 4 c-terminal amino acids. kcat: 0.174/sec (phosphoenolpyruvate), 0.14% wild type catalytic activity
G961A
kcat: 17.4/sec (phosphoenolpyruvate), 24.3% of wild type catalytic activity
G961V
kcat: 7.2/sec (phosphoenolpyruvate), 8.5% of wild type catalytic activity
S8C
Sorghum sp.
-
he S-carboxymethylated S8C mutant enzyme, in contrast to the SH-modified wild type protein, has an increased I0.5 value for L-malate similar to that of the phosphorylated Ser8 enzyme and the S8D mutant protein
E954K
mutation renders the enzyme sensitive to inhibition by malate, aspartate, and fumarate
S967V
loss of activity
D228N
-
reduced apparent affinity for the activator glycine
E229A
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is lower than wild-type value
R183Q
-
mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected
R183Q/R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R226Q
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is significantly higher than that of wild-type enzyme
R231A
-
decreased apparent affinity for the activator glucose 6-phosphate
R232Q
-
decreased apparent affinity for the activator glucose 6-phosphate, reduced apparent affinity for the activator glycine
R372Q
-
mutation results in a marked decrease in sensitivity to glucose 6-phosphate
additional information