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
Metals Ions
Metals Ions on EC 2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
-
can partially replace Mg2+
Fe2+
6% activity in the presence of Mn2+ compared to Mg2+
K+
-
monovalent cation required, K+, Li+ or NH4+ markedly stimulate
Li+
-
monovalent cation required, K+, Li+ or NH4+ markedly stimulate
NH4+
-
monovalent cation required, K+, Li+ or NH4+ markedly stimulate
Zn2+
-
can partially replace Mg2+
additional information
not stimulated by Ca2+, Zn2+, and Cu2+
Co2+
12% activity in the presence of Mn2+ compared to Mg2+
Co2+
-
can partially replace Mg2+
Mg2+
-
maximal activity at 0.1-0.2 mM
Mg2+
-
absolute requirement for a divalent metal ion, Mg2+ is most effective, optimal activity at 1.5 mM
Mg2+
-
divalent cation required, Km: 0.2 mM
Mg2+
the enzyme requires bivalent metal ions and its activity is highest in the presence of Mg2+
Mg2+
required for activity, 6 mM used in assay conditions
Mg2+
-
absolute requirement
Mg2+
-
divalent cation required, Mg2+ is most effective at 1 mM
Mg2+
-
absolute requirement for divalent cations. Mg2+ is most effective. Optimal concentrations are 4, 6 and 10 mM for 20, 40 and 100 mM sodium acetate/acetic acid buffer, pH 5.5
Mg2+
-
absolute requirement. Optimal concentration is 1 mM in absence of ATP and 7 mM in presence of ATP at 5 mM
Mg2+
-
optimal Mg2+ concentration: 1 mM
Mn2+
-
half as effective as Mg2+
Mn2+
-
at 1 mM, 80% of the activation with Mg2+
Mn2+
27% activity in the presence of Mn2+ compared to Mg2+
Mn2+
-
0.3 mM, can fully replace Mg2+