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ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
ATP + H2O
ADP + phosphate
-
-
-
?
additional information
?
-
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
catalyzes the aspartate addition at the alpha-amino group to the growing purine backbone
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
-
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
rapid equilibrium random ter-ter mechanism
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
-
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
r
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
in the reverse reaction phosphate can be replaced by arsenate
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
in the reverse reaction ADP cannot be replaced by any of the other nucleoside diphosphates
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
-
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
Pigeon
-
-
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
ADP + phosphate + 1-(5'-phosphoribosyl)-5-amino-4-(N-succinocarboxamide)-imidazole
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
bifunctional enzyme having also 5-aminoimidazole ribonucleotide carboxylase, i.e. AIRc, activity
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
seventh of ten steps in the purine biosynthesis, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
ligation of the carboxylate group of CAIR to the amino group of aspartate
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
ATP in form of MgATP2-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) is an important bifunctional enzyme in de novo purine biosynthesis in vertebrate with both 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase (SAICARs) activities
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
?
additional information
?
-
usage of the malachite green assay screening method for detection of inhibitors of SAICAR synthetase (PurC). A gradual increase in inaorganic phosphate occurs in positive control samples over the course of the day. Further investigation indicates that hydrolysis of ATP catalyzed by PurC, rather than substrate-related phosphate release, is responsible for a partial contribution to the signals in the control samples. Thus substrate-independent ATPase activity may complicate high throughput screening
-
-
-
additional information
?
-
-
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
?
additional information
?
-
-
in higher organisms PurC and PurE are fused to form a bifunctional enzyme, overview, active site structure, overview
-
-
?
additional information
?
-
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
?
additional information
?
-
-
in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
catalyzes the aspartate addition at the alpha-amino group to the growing purine backbone
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
ATP + 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole + L-Asp
?
-
one of the enzymes of the series involved in the biosynthesis of the purine nucleotides de novo
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
seventh of ten steps in the purine biosynthesis, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) is an important bifunctional enzyme in de novo purine biosynthesis in vertebrate with both 5-aminoimidazole ribonucleotide carboxylase (AIRc) and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase (SAICARs) activities
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
seventh of ten steps in the purine biosynthesis, pathway overview
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
-
?
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
ADP + phosphate + (S)-2-[5-amino1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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metabolism
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase (PurC) is a key enzyme in the de novo purine biosynthetic pathway of bacteria
metabolism
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase (PurC) is a key enzyme in the de novo purine biosynthetic pathway of bacteria
metabolism
-
increased expression of the enzymes of de novo purine biosynthetic pathway in lung adenocarcinomas, phosphoribosyl amidotransferase (PPAT), phosphoribosylaminoimidazole carboxylase, and phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS). Modulation of PPAT and PAICS or glutamine treatment alters pyruvate kinase (PK) activity, overview
metabolism
the enzyme is involved in the purine nucleotide metabolism, catalyzing the formation pf a pecursor of cordycepin
metabolism
-
the seventh step of the de novo purine-biosynthesis pathway converts carboxyaminoimidazoleribonucleotide (CAIR) and L-aspartic acid (Asp) to 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide (SAICAR) in the presence of adenosine 5'-triphosphate (ATP) using the enzyme PurC
metabolism
SAICAR synthetase (PurC) is involved in de novo purine biosynthesis
metabolism
-
the seventh step of the de novo purine-biosynthesis pathway converts carboxyaminoimidazoleribonucleotide (CAIR) and L-aspartic acid (Asp) to 4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide (SAICAR) in the presence of adenosine 5'-triphosphate (ATP) using the enzyme PurC
-
metabolism
-
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase (PurC) is a key enzyme in the de novo purine biosynthetic pathway of bacteria
-
metabolism
-
the enzyme is involved in the purine nucleotide metabolism, catalyzing the formation pf a pecursor of cordycepin
-
physiological function
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Zygotic paics mutants have pigmentation defects in which xanthophore and iridophore pigmentation is almost completely absent, and melanin-derived pigmentation is significantly decreased, even though pigment cells are present in normal amounts and distributions. Zygotic paics mutants are also microphthalmic, resulting from defects in cell cycle exit of proliferative retinoblasts within the developing eye. Maternal-zygotic and maternal-effect mutants demonstrate a crucial requirement for maternally derived paics, these mutants show more severe developmental defects than their zygotic counterparts
physiological function
the enzyme is involved in the de novo purine biosynthesis pathway
physiological function
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enzyme phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) produces the intermediary metabolite N-succinyl-5-aminoimidazole-4-carboxamide-1-ribose-5'-phosphate (SAICAR), known to activate pyruvate kinase isoform PKM2 under glucose-depleted condition. Increased expression of the enzymes of de novo purine biosynthetic pathway in lung adenocarcinomas, phosphoribosyl amidotransferase (PPAT), phosphoribosylaminoimidazole carboxylase, and PAICS. PAICS shows increased expression with disease progression and is significantly associated with poor prognosis. Altering PPAT and PAICS expression modulates pyruvate kinase activity, cell proliferation and invasion. Regulation of both PPAT and PAICS and pyruvate kinase activity by L-glutamine, a co-substrate for PPAT. PPAT and PAICS genes are necessary for lung tumorigenesis
physiological function
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enzyme PurC is conditionally essential for bacterial replication
physiological function
the enzyme catalyzes direct activation of the carboxylate of CAIR by the gamma-phosphate of ATP, leading to the formation of products, SAICAR, ADP and phosphate
physiological function
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enzyme PurC is conditionally essential for bacterial replication
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physiological function
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the enzyme is involved in the de novo purine biosynthesis pathway
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additional information
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bifunctional enzyme complex, termed PAICS, harboring 5-aminoimidazole ribonucleotide carboxylase and 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase activities, the SAICAR active sites is located in the N-terminal domain of PAICS, structure modeling, overview. In addition to the basic loop responsible for phosphate-binding, the adenine-ribose moiety of the nucleotide sits in a largely hydrophobic pocket sandwiched between beta1-strands of the SAICAR domain
additional information
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structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
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structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
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structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview
additional information
analysis of the dimer structure of enzyme SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview
additional information
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analysis of the dimer structure of enzyme SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview
additional information
modeling of the quaternary structure of dimeric enzyme BaPurC, based on the dimer structure of Streptococcus pneumoniae SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview
additional information
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modeling of the quaternary structure of dimeric enzyme BaPurC, based on the dimer structure of Streptococcus pneumoniae SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview
additional information
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modeling of two structures for the active site with all of the essential ligands (ATP, Mg2+, Asp and CAIR) and of a relay mechanism for the formation of the product (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate (SAICAR), active site structure analysis, overview
additional information
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modeling of two structures for the active site with all of the essential ligands (ATP, Mg2+, Asp and CAIR) and of a relay mechanism for the formation of the product (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate (SAICAR), active site structure analysis, overview
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additional information
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analysis of the dimer structure of enzyme SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview
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hanging-drop vapor diffusion, crystal structures of the ADP and the ADP/4-carboxy-5-aminoimidazole ribonucleotide complexes of SAICAR synthetase. ADP and 4-carboxy-5-aminoimidazole ribonucleotide bind to the active site in association with three Mg2+, two of which coordinate the same oxygen atom of the 4-carboxyl group of CAIR, whereas, the third coordinates the alpha- and beta-phosphoryl groups of ADP. The polypeptide fold for residues 204-221 of the Escherichia coli structure differs significantly from those of the ligand-free SAICAR synthetase from Thermatoga maritima and the adenine nucleotide complexes of the synthetase from Saccharomyces cerevisiae
the 2.8 A resolution structure reveals that eight PAICS subunits, each composed of distinct AIRc and SAICARs domains, assemble a compact homo-octamer with an octameric-carboxylase core and four symmetric periphery dimers formed by synthetase domains
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co-crystallization of SAICAR synthetase from Pyrococcus horikoshii with substrates and other nucleotides produces eight ligand bound structures, five in C2221 and three in H3 space groups. These ligand bound complexes have minor structural deviations compared to their corresponding apo structures. In most of the structures the hydrolyzed product of the nucleotide triphosphates are bound to the enzyme
space group P31, presence of a hexamer in the asymmetric unit
crystals of SAICAR complexed with 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and succinic acid are grown by hanging drop vapor diffusion at room temperature, mother liquor consists of 24 mg/ml SAICAR, 1 M ammonium sulfate, 100 mM 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide, 100 mM succinic acid and 50 mM Tris-HCl, pH 7.5, crystals diffract to 1.3 A
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hanging drop vapor diffusion, drops contain protein at a concentration of 8-15 mg/ml in 50 mM Tris-HCl, pH 7.0, 40 mM aspartic acid and 1.0-1.25 M ammonium sulfate, crystals diffract to 1.9 A resolution
hanging-drop vapor-diffusion method. Crystals of the complex of the enzyme SAICAR synthase with the reaction product belong to space group P2(1)2(1)2(1) containing one molecule per asymmetric unit
purified recombinant His-tagged enzyme complexed with ADP or ADP, L-Asp and 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, hanging drop vapour diffusion method, mixing of 0.002 ml of 0.25 mM protein in 15 mM Tris, pH 8.0, 25 mM KCl, 55 mM MgCl2, 5 mM EDTA, and 5 mM DTT, with 0.002 ml of reservoir solution containing 0.16 M sodium acetate, pH 4.5, 36-40% w/v PEG 200, plus mM ADP, 1 mM CAIR, and 4 mM Asp or plus 10 mM ADP, X-ray diffraction structure determination and analysis at 2.3-2.69 A resolution, modeling, molecular replacement using the Escherichia coli enzyme structure, PDB ID 2gqr, as search model
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to 2.8 A resolution, space group P2
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hanging-drop vapor-diffusion conditions, 2.2 A resolution crystal structure. Protein structure is described and compared with that of the ATP-SAICAR synthase complex from yeast
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purified enzyme in 150 mM NaCl, 1 mM DTT, 10 mM HEPES-KOH, pH 7.5, is mixed with 50 mM Tris pH 8.0, 2M ammonium sulfate and 1% PEG400, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling
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