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2.5.1.72: quinolinate synthase

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

Word Map on EC 2.5.1.72

Reaction

glycerone phosphate
+
iminosuccinate
=
pyridine-2,3-dicarboxylate
 + 2 H2O +
phosphate

Synonyms

Fe4S4 quinolinate synthase, NadA, Old5, PfQS, quinolinate synthetase, SufE3, TM_1644

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.72 quinolinate synthase

Engineering

Engineering on EC 2.5.1.72 - quinolinate synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C110S
-
0.4 mol iron per mol of protein, no enzymic activity
C230S
-
0.6 mol iron per mol of protein, no enzymic activity
C259S
-
4.5 mol iron per mol of protein, 80% of wild-type activity
C318S
-
3.3 mol iron per mol of protein, 75% of wild-type activity
C318S/C320S
-
0.3 mol iron per mol of protein, no enzymic activity
C320S
-
1.5 mol iron per mol of protein, no enzymic activity
C82S
-
4.3 mol iron per mol of protein, activity similar to wild-type
C113A
C113S
-
1.3 iron ions per polypeptide, no catalytic activity
C119A
-
2.9 mol of iron and sulfur per mol of protein
C119S
-
1.0 iron ions per polypeptide
C128S
-
2.7 iron ions per polypeptide
C195S
-
1.5 iron ions per polypeptide
C200A
C200S
-
1.0 iron ions per polypeptide, no catalytic activity
C291A
-
3.9 mol of iron and sulfur per mol of protein
C291A/C294A
-
3.7 mol of iron and sulfur per mol of protein
C291A/C294A/C297A
-
0.5 mol of iron and sulfur per mol of protein
C291S
-
0.8 iron ions per polypeptide
C294A
-
3.2 mol of iron and sulfur per mol of protein
C294A/C297A
-
0.6 mol of iron and sulfur per mol of protein
C294S
-
2.1 iron ions per polypeptide
C297A
C297S
-
0.3 iron ions per polypeptide, no catalytic activity
C64S
-
1.4 iron ions per polypeptide
E198Q
-
site-directed mutagenesis, inactive mutant
Y109F
-
site-directed mutagenesis, inactive mutant
Y23F
-
site-directed mutagenesis, inactive mutant
K219R
mutant is able to bind citrate
K219R/Y107F
crystallization data. The mutated protein is unable to catalyze the aldo-keto isomerization and/or cyclization of the first intermediate resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate that ultimately leads to quinolinic acid formation
K219R/Y21F
crystallization data
Y21F
mutant is able to bind citrate
Y21F/K219R
crystallization data with inhibitors
K219R
-
mutant is able to bind citrate
-
K219R/Y107F
-
crystallization data. The mutated protein is unable to catalyze the aldo-keto isomerization and/or cyclization of the first intermediate resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate that ultimately leads to quinolinic acid formation
-
K219R/Y21F
-
crystallization data
-
Y21F
-
mutant is able to bind citrate
-
Y21F/K219R
-
crystallization data with inhibitors
-
additional information