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1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
2-deoxy-D-ribose 5-phosphate
-
92% inhibition at 1 mM
5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethoxy)adenine
9-(2-phosphonylmethoxyethyl)adenine
adenosine 5'-(beta,gamma-imido)-triphosphate
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inhibition at 1 mM
allopurinol ribonucleotides
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23% inhibition at 1 mM
alpha,beta-methylene ATP
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D-fructose 1,6-diphosphate
D-ribose 1-phosphate
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13% inhibition at 1 mM
dATP
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inhibition at 1 mM
diadenosine pentaphosphate
Inhibits the dephosphorylation of ATP and ADP by nonspecific phosphatases.
DL-1,4-Anhydroribitol 5-phosphate
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competitive inhibition to D-ribose-5-phosphate
FAD
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51% inhibition at 1 mM
glyceraldehyde 3-phosphate
GSH
-
marked inhibition of enzyme in crude extract at 1 mM
IMP
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21% inhibition at 1 mM
Mn2+
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complete inhibition above 0.4 mM
NAD+
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100% inhibition at 1 mM
NADH
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72% inhibition at 1 mM
NADPH
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100% inhibition at 1 mM
PRPP synthetase-associated proteins
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SO42-
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1 M, strong inhibition
TTP
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47% inhibition at 1 mM
XDP
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36% inhibition at 1 mM
XTP
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22% inhibition at 1 mM
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
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mixed-type inhibition with respect to D-ribose 5-phosphate and no inhibition against ATP
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
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at pH 7.5, competitive inhibition with respect to D-ribose 5-phosphate and noncompetitive inhibition with respect to ATP
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
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at pH 7.5, competitive inhibition with respect to D-ribose 5-phosphate and noncompetitive inhibition with respect to ATP
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
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partial noncompetitive inhibition with respect to D-ribose 5-phosphate and no inhibition with respect to ATP
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
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partial mixed-type inhibition with respect to D-ribose 5-phosphate and ATP
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
-
2,3-diphosphoglycerate
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competitive to D-ribose 5-phosphate; inhibition of the erythrocyte enzyme
2,3-diphosphoglycerate
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30% inhibition at 1 mM; competitive to D-ribose 5-phosphate
2,3-diphosphoglycerate
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at 1 mM, inhibition of isoenzyme PRSI and PRSII, at 1-10 mM, stimulation of isoenzyme PRSI
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
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inhibition, even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol
5-phospho-alpha-D-ribose 1-diphosphate
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competitive with respect to ATP and noncompetitive with respect to D-ribose 5-phosphate
5-phospho-alpha-D-ribose 1-diphosphate
-
-
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive to ribose 5-phosphate
5-phospho-alpha-D-ribose 1-diphosphate
-
-
5-phospho-alpha-D-ribose 1-diphosphate
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competitive with respect to ATP and noncompetitive with respect to D-ribose 5-phosphate
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of 0.86 mM
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of more than 2.5 mM
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 1.9 mM
9-(2-phosphonylmethoxyethyl)adenine
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IC50 of 2.1 mM
adenosine
-
no inhibition
adenosine
-
27% inhibition at 1 mM
ADP
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ADP
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allosterical inhibition
ADP
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nonlinear competitive inhibition
ADP
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competitive inhibition to ATP
ADP
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99% inhibition at 1 mM; competitive inhibition to ATP; end product inhibition; the most effective
ADP
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even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol; the most effective
ADP
allosterical inhibition
ADP
a single ADP binding site, the active site, is present per subunit
ADP
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competitive inhibition to ATP
ADP
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one of the most effective
ADP
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the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells
ADP
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one of the most effective
ADP
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when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
ADP
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one of the most effective
ADP
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non competitive with respect to ATP at 0.2 mM D-ribose-5-phosphate; the most effective
ADP
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competitive inhibition to ATP
ADP
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inhibits isoenzymes PRS1 and PRS2 efficiently, but not isoenzymes PRS3 and PRS4
ADP
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at low concentrations ADP inhibition is linearly competitive with respect to ATP. Less than 1% residual activity in presence of 5 mM ADP
alpha,beta-methyleneATP
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competitive inhibition to ATP
alpha,beta-methyleneATP
-
competitive inhibition to ATP
AMP
-
68% inhibition at 5 mM
AMP
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noncompetitive with respect to D-ribose 5-phosphate and competitive with respect to ATP
AMP
-
69% inhibition at 1 mM
AMP
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noncompetitive to both substrates
AMP
-
one of the most effective
AMP
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the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
AMP
-
one of the most effective
AMP
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non competitive with respect to D-ribose 5-phosphate and ATP
AMP
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noncompetitive to both substrates
ATP
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moderate inhibition above 3 mM
ATP
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free form, slight inhibition at 1 mM
ATP
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free form, slight inhibition at 1 mM
Ca2+
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inhibition even in presence of excess Mg2+
Ca2+
-
inhibition even in presence of excess Mg2+
Ca2+
-
IC50 of 0.05 mM; inhibition even in presence of excess Mg2+
Ca2+
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low concentrations of CaCl2 in the presence of an excess of MgCl2 result in a reduction in catalytic activity. At CaCl2 1 mM, the enzyme is less sensitive to ADP inhibition
CDP
-
44% inhibition at 1 mM
CTP
-
40% inhibition at 1 mM
CTP
-
weak inhibition at 1 mM
CTP
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the most effective pyrimidine nucleotide inhibitor
Cu2+
-
-
D-fructose 1,6-diphosphate
-
no inhibition
D-fructose 1,6-diphosphate
-
20% inhibition at 1 mM
D-fructose 1,6-diphosphate
-
no inhibition
D-Fructose 1-phosphate
-
19% inhibition at 1 mM
D-Fructose 1-phosphate
-
no inhibition
D-ribose 5-phosphate
-
-
D-ribose 5-phosphate
-
at unsaturating phosphate concentrations
D-ribose 5-phosphate
-
substrate inhibition above 1.5 mM
D-ribose 5-phosphate
-
inhibition in presence of Ca2+, without ADP; substrate inhibition in presence of ADP, not in its absence
D-ribose 5-phosphate
-
substrate inhibition in presence of ADP, not in its absence
D-ribose 5-phosphate
-
inhibition in presence of Ca2+, without ADP; substrate inhibition in presence of ADP, not in its absence
dADP
-
competitive to ATP
dADP
-
induces substrate inhibition by D-ribose-5-phosphate
GDP
-
GDP
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64% inhibition at 5 mM
GDP
-
even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol
GDP
-
the enzyme is weakly sensitive to GDP
GDP
50% residual activity at 5 mM
GDP
-
one of the most effective
GDP
-
when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
GDP
-
one of the most effective
GDP
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below 3-4 mM, linear competitive inhibition with respect to ATP
GDP
-
5 mM, less than 1% residual activity
glyceraldehyde 3-phosphate
-
no inhibition
glyceraldehyde 3-phosphate
-
14% inhibition at 1 mM
GMP
-
88% inhibition at 5 mM
GMP
-
27% inhibition at 1 mM
GTP
-
no inhibition
GTP
-
51% inhibition at 1 mM
GTP
-
weak inhibition at 1 mM
GTP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
GTP
-
substrate inhibition
guanosine
-
no inhibition
guanosine
-
20% inhibition at 1 mM
IDP
-
47% inhibition at 1 mM
IDP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
ITP
-
36% inhibition at 1 mM
ITP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
L-histidine
-
no inhibition
L-histidine
-
no inhibition
L-histidine
-
weak inhibition or no inhibition
L-histidine
-
no inhibition
L-histidine
-
no inhibition
L-tryptophan
-
no inhibition
L-tryptophan
-
no inhibition
L-tryptophan
-
weak inhibition or no inhibition
L-tryptophan
-
no inhibition
L-tryptophan
-
no inhibition
nucleotides
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-
-
nucleotides
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enzyme from HTC cells has an altered sensitivity to feedback inhibition by purine and pyrimidine nucleotides
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nucleotides
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nucleoside tri- and diphosphates are more effective than nucleoside monophosphates, ribonucleotides more effective than deoxynucleotides; purines more effective than pyrimidines
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nucleotides
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purines more effective than pyrimidines
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phosphate
-
inhibition at low concentrations of D-ribose 5-phosphate
phosphate
-
inhibition at high concentrations, more pronounced in the reverse reaction
phosphate
-
IC50 of 28 mM
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
TDP
-
100% inhibition at 1 mM
TDP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
UDP
-
no inhibition
UDP
-
10%-16% inhibition at 1 mM
UDP
-
10%-16% inhibition at 1 mM
UDP
-
10%-16% inhibition at 1 mM
UMP
-
no inhibition
UMP
-
10%-18% inhibition at 1 mM
UMP
-
10%-18% inhibition at 1 mM
UTP
-
no inhibition
UTP
-
weak inhibition at 1 mM
UTP
-
substrate inhibition
UTP
-
5.0 mM, significant inhibition
additional information
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D-glucose-6-phosphate have no effects on the enzyme activity; dihydroxyacetone phosphate, D-glucose-1-phosphate, fructose-6-phosphate, ribose, sucrose, glutamine, glutamic acid, aspartic acid, alanine, alpha-ketoglutarate, pyruvate, citrate, malate, fumarate, succinate, cytidine, uridine, adenine, orotate, guanine, cytosine and xanthine have no effects on the enzyme activity
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additional information
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-
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additional information
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inhibition by pair of inhibitors tested is not greater than the sum of the inhibition produced by each alone
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additional information
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pyrimidine, pyridine and purine nucleotides and reaction products
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additional information
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no inhibitory effects are shown by the presence of pyrimidine nucleoside mono- or diphosphates or of histidine, up to 2 mM
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additional information
the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride
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additional information
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the enzyme activity is not affected by the presence of 8 M urea or 4 M guanidinium chloride
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additional information
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-
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additional information
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native enzyme is less sensitive to nucleotide inhibition than the major component of the enzyme, rPRSI
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additional information
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GSH, 2-mercaptoethanol, 2,3-dimercaptopropanol, dithiothreitol, at 1 mM, have no effect or slightly inhibit the highly purified enzyme
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additional information
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purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
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additional information
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Ba2+, Fe2+, Mn2+ and Zn2+ do not inhibit at concentrations below 1 mM; purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
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additional information
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6-phosphogluconate, 3-phosphoglycerate, phosphoenolpyruvate and ribulose-5-phosphate have no effect on the activity; D-glucose-6-phosphate have no effects on the enzyme activity; purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
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