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2.4.2.19: nicotinate-nucleotide diphosphorylase (carboxylating)

This is an abbreviated version!
For detailed information about nicotinate-nucleotide diphosphorylase (carboxylating), go to the full flat file.

Word Map on EC 2.4.2.19

Reaction

beta-nicotinate D-ribonucleotide
+
diphosphate
 +
CO2
=
pyridine-2,3-dicarboxylate
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

BNA6, general stress protein 70 , GSP70 , Hp-QAPRTase, hQPRTase, M6_Spy1061, NAD pyrophosphorylase, NadC, nicotinate mononucleotide pyrophosphorylase (carboxylating) (EC 2.4.2.19), nicotinate-nucleotide pyrophosphorylase (carboxylating), nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase (decarboxylating), pyrophosphorylase, nicotinate mononucleotide (carboxylating), QAPRTase, QPRT, QPRTase, QPRTase , QPT, QPT1, QPT2, quinolate phosphoribosyltransferase, quinolinate phosphoribosyl transferase, quinolinate phosphoribosyltansferase, quinolinate phosphoribosyltransferase, quinolinate phosphoribosyltransferase (decarboxylating), quinolinate phosphoribosyltransferase 1, quinolinate phosphoribosyltransferase 2, quinolinate phosphoribosyltransferase [decarboxylating] , quinolinic acid phosphoribosyl transferase, quinolinic acid phosphoribosyltransferase, quinolinic phosphoribosyltransferase, sp.NadC, spNadC, TM1645, type II quinolic acid phosphoribosyltransferase, type II quinolinic acid phosphoribosyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.19 nicotinate-nucleotide diphosphorylase (carboxylating)

Engineering

Engineering on EC 2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K139A
inactive, K139 is part of quinolinic acid binding site
K139S
inactive, K139 is part of quinolinic acid binding site
K171A
inactive, K171 is part of quinolinic acid binding site
K171S
inactive, K171 is part of quinolinic acid binding site
R102A
10% remaining activity, R102 is part of quinolinic acid binding site, denotes from the other subunit in the canonical dimer
R102Q
10% remaining activity, R102 is part of quinolinic acid binding site, denotes from the other subunit in the canonical dimer
R138Q
inactive, R138 is part of quinolinic acid binding site
R161A
R161Q
inactive, R161 is part of quinolinic acid binding site
D235A
-
does not affect ligand binding or catalysis, KD value for quinolinic acid is similar to wild-type, increases KD value for 5-phospho-alpha-D-ribose 1-diphosphate by 2fold
E214A
-
increases KD value for quinolinic acid by 2fold and for 5-phospho-alpha-D-ribose 1-diphosphate by 15fold, causes at least a 4000fold reduction in kcat. Presence of benzene-1,2-dicarboxylic acid results in 3.4fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding
E214D
-
KD value for quinolinic acid is similar to wild-type, increases KD value for 5-phospho-alpha-D-ribose 1-diphosphate by 10fold. Presence of benzene-1,2-dicarboxylic acid results in 6fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding
E214Q
-
increases KD value for quinolinic acid by 2fold and for 5-phospho-alpha-D-ribose 1-diphosphate by 2fold, has only modest effects on ligand binding and catalysis, wild-type-like pH profile. Presence of benzene-1,2-dicarboxylic acid results in 2fold tightening of 5-phospho-alpha-D-ribose 1-diphosphate binding
K153A
-
inactive enzyme, kcat value decreases by more than 4000fold, is able to bind quinolinic acid with a KD value 2fold higher than that of wild-type
K185A
-
kcat value is reduced by 625fold, and binding affinity of quinolinic acid and 5-phospho-alpha-D-ribose 1-diphosphate to the enzyme decreases. Displays 83fold increase in activity toward the normally inactive quinolinic acid analogue, nicotinic acid. Displays a 300fold higher kcat/Km for nicotinic acid over the natural substrate quinolinic acid
K284A
-
KD value for quinolinic acid is similar to wild-type, decreases kcat by 30fold and increases Km and KD values for 5-phospho-alpha-D-ribose 1-diphosphate by 80fold and at least 20fold, respectively
R118A
-
results in 5000fold decrease in kcat value and a decrease in the binding affinity of quinolinic acid and 5-phospho-alpha-D-ribose 1-diphosphate to mutant R152A. Equimolar mixtures of mutant R118A with inactive or virtually inactive mutants produce approximately 50% of the enzymatic activity of wild-type
R152A
-
kcat value is reduced by 33fold, and binding affinity of quinolinic acid and 5-phospho-alpha-D-ribose 1-diphosphate to the enzyme decreases. Displays 116fold increase in activity toward the normally inactive quinolinic acid analogue, nicotinic acid
additional information
-
mutants can use 6-aminonicotinic acid as substrate, whereas 2,4-pyridinedicarboxylic acid, 2,5-pyridinedicarboxylic acid, 2,6-pyridinedicarboxylic acid, 3,4-pyridinedicarboxylic acid, 3,5-pyridinedicarboxylic acid, nicotinamide and pyridine-4-carboxylic acid are not utilized by the mutant enzymes