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2,6-diaminopurine
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competitive
4-aminopyrido(2,3-d)pyrimidine
-
-
4-aminopyrolo(2,3-d)pyrimidine
-
-
6-Mercaptopurine
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competitive
alpha-D-5-phosphoribose 1-diphosphate
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substrate inhibition
benznidazole
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transcriptome and functional genomics reveal the participation of adenine phosphoribosyltransferase in Trypanosoma cruzi resistance to benznidazole
benzyladenine
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competitive
D-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate
D-DIAB, a iminoaltritol bis-phosphate, transition-state analogue inhibitor, enzyme interactions and binding structure analysis
EDTA
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reversible by 2-mercaptoethanol and excess Mg2+
formycin AMP
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competitive against adenine and diphosphate
immucillin AB
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does not bind at the active site
isodutaduprine
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alkaloid from Almeidea rubra, 21.6% inhibition at 0.0356 mM of the recombinant enzyme
isokokusagine
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alkaloid from Almeidea rubra, 44.6% inhibition at 0.0412 mM of the recombinant enzyme
isoskimmianine
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alkaloid from Almeidea rubra, 39.1% inhibition at 0.0386 mM of the recombinant enzyme
L-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate
L-DIAB, a iminoaltritol bis-phosphate, enzyme binding structure analysis
adenine
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-
adenine
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substrate inhibition, 0.08 mM, 50% inhibition in Propositus (HPRT-) and 20% in control(HPRT+)
adenine
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at high concentrations, at low 5-phospho-alpha-D-ribose 1-diphosphate concentration
ADP
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-
ADP
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is a much stronger inhibitor than ATP at pH 4.5, but has virtually no effect on activity at neutral pH
ADP
the inhibitor binds like the product AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site
AMP
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-
AMP
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competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
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competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
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competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate; competitive against adenine
AMP
-
2 mM, 80% inhibition with Propositus (HPRT-) and 58% in control(HPRT+)
AMP
5-phospho-alpha-D-ribose 1-diphosphate and AMP compete for the same site where the latter also acts as a competitive inhibitor of the forward reaction. Tyr105 prevents strong inhibition of hAPRT by AMP
AMP
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competitive against 5-phospho-alpha-D-ribose 1-diphosphate
ATP
-
-
Ba2+
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in presence of MnCl2
Ca2+
-
in presence of MnCl2
Ca2+
-
activation, competitive to Mg2+
Cd2+
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in presence of MnCl2
diphosphate
-
-
diphosphate
noncompetitive against 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate
-
no inhibition
diphosphate
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competitive against adenine and 5-phosphoribose 1-diphosphate
GMP
-
-
guanine
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noncompetitive against 5-phosphoribose 1-diphosphate
Hg2+
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in presence of MnCl2
Hg2+
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reversed by 2-mercaptoethanol
Hg2+
-
complete inhibition at 5 mM
Mg2+
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inhibition in presence of MnCl2, activation in absence
Mg2+
-
inhibition above 2 mM, activation below
Mg2+
required, high concentration of Mg2+ inhibited the reaction with a Ki = 5.4 mM
Mg2+
-
inhibitory effects are noncompetitive against 5-phosphoribose 1-diphosphate
N-ethylmaleimide
-
-
N-ethylmaleimide
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strong, DTT or glutathione protect
N-ethylmaleimide
-
no inhibition
Na+
-
no inhibition
nucleotides
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higher concentrations of all 5'-nucleotides are most inhibitory, 6-OH purine nucleotides are moderately inhibitory, pyrimidine nucleotides are least inhibitory
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nucleotides
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effect is strongly influenced by pH, inhibition at pH 7.1: ATP, GMP, activation at pH 7.1: GTP, UMP, UTP, CMP, CTP, IMP, no effect at pH 7.1: AMP, inhibition at pH 8.0: AMP, ATP, GMP, GTP, UTP, CTP, IMP, no effect at pH 8.0: UMP, CMP
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nucleotides
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nucleotide mono-, di- and triphosphates of adenine, guanine and hypoxanthine
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nucleotides
-
effect is strongly influenced by pH, inhibition at pH 7.1: ATP, GMP, activation at pH 7.1: GTP, UMP, UTP, CMP, CTP, IMP, no effect at pH 7.1: AMP, inhibition at pH 8.0: AMP, ATP, GMP, GTP, UTP, CTP, IMP, no effect at pH 8.0: UMP, CMP
-
p-chloromercuribenzoate
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complete inhibition at 1 mM, DTT or glutathione protect
p-chloromercuribenzoate
-
no inhibition
p-chloromercuribenzoate
-
no inhibition
p-chloromercuribenzoate
-
reversed by 2-mercaptoethanol and excess Mg2+
p-hydroxymercuribenzoate
-
DTT
p-hydroxymercuribenzoate
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not enzyme from monkey liver
Pb2+
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inhibits the enzyme in erythrocytes about 25% at 0.0005 mM and about 20% at 0.0001 mM, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, APRT inhibition as one of the mechanisms of lead toxicity
Pb2+
-
moderately inhibits both the enzyme in erythrocytes even at very low concentrations, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, APRT inhibition as one of the mechanisms of lead toxicity
SO42-
-
no inhibition
sulfhydryl reagents
-
-
Zn2+
-
-
additional information
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no substrate inhibition by adenine
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additional information
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no effect of a variety of sugars, amino acids, organic acids and nucleotides tested, except for AMP, have any effect on the enzyme activity; not affected by PO43-
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additional information
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methanolic and hexanic extracts from roots and leaves of Cedrela fissilis and from fruits, branches and leaves of Cipadessa fruticosa show strong antileishmanicidal activities, the inhibitory activities of plant organ extracts with dichloromethane are lower, overview
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additional information
not inhibited by Ocimum basilicum leaf essential oil
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additional information
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not affected by 2,6-diaminopurine, 4-carbamoylimidazolium 5-olate, 8-azaadenine, and 2-fluoro-6-aminopurine
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additional information
expression of gene OsAPT2 is temperature-sensitive and is downregulated at 29°C
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additional information
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expression of gene OsAPT2 is temperature-sensitive and is downregulated at 29°C
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additional information
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no inhibition by iodoacetamide, DTNB
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additional information
an enantiomeric pair of iminoaltritol bis-phosphates (L-DIAB and D-DIAB) is synthesized and shown to display inhibition of Saccharomyces cerevisiae adenine phosphoribosyltransferase (ScAPRT). Synthesis pathway, detailed overview. Crystallographic inhibitor binding analysis of L- and D-DIAB bound to the catalytic sites of ScAPRT demonstrates accommodation of both enantiomers by altered ring geometry and bis-phosphate catalytic site contacts
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additional information
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an enantiomeric pair of iminoaltritol bis-phosphates (L-DIAB and D-DIAB) is synthesized and shown to display inhibition of Saccharomyces cerevisiae adenine phosphoribosyltransferase (ScAPRT). Synthesis pathway, detailed overview. Crystallographic inhibitor binding analysis of L- and D-DIAB bound to the catalytic sites of ScAPRT demonstrates accommodation of both enantiomers by altered ring geometry and bis-phosphate catalytic site contacts
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additional information
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mechanism of product inhibition; no inhibition by GMP, XMP, UMP, CMP, and CDP
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