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Literature summary extracted from

  • Zhang, Y.; Morar, M.; Ealick, S.E.
    Structural biology of the purine biosynthetic pathway (2008), Cell. Mol. Life Sci., 65, 3699-3724.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.6 Mg2+
-
Escherichia coli
6.3.2.6 Mg2+
-
Homo sapiens
6.3.2.6 Mg2+
-
Thermotoga maritima
6.3.2.6 Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate Homo sapiens PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate Escherichia coli seventh of ten steps in the purine biosynthesis, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate Thermotoga maritima seventh of ten steps in the purine biosynthesis, pathway overview ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate Saccharomyces cerevisiae seventh of ten steps in the purine biosynthesis, pathway overview ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.6 Escherichia coli
-
gene purC
-
6.3.2.6 Homo sapiens
-
gene purCE
-
6.3.2.6 Saccharomyces cerevisiae P27616 gene purC
-
6.3.2.6 Thermotoga maritima
-
gene purC
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
-
Homo sapiens ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR ?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
-
Thermotoga maritima ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR ?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
-
Saccharomyces cerevisiae ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR ?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate PurCE performs the sixth and seventh of ten steps in the purine biosynthesis, pathway overview Homo sapiens ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate seventh of ten steps in the purine biosynthesis, ligation of the carboxylate group of CAIR to the amino group of aspartate, pathway overview Escherichia coli ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate seventh of ten steps in the purine biosynthesis, pathway overview Thermotoga maritima ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate seventh of ten steps in the purine biosynthesis, pathway overview Saccharomyces cerevisiae ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
?
6.3.2.6 ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate ligation of the carboxylate group of CAIR to the amino group of aspartate Escherichia coli ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate i.e. N-succinocarboxamide-5-aminoimidazole ribonucleotide or SAICAR ?
6.3.2.6 additional information in higher organisms PurC and PurE are fused to form a bifunctional enzyme, overview, active site structure, overview Homo sapiens ?
-
?
6.3.2.6 additional information in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview Escherichia coli ?
-
?
6.3.2.6 additional information in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview Thermotoga maritima ?
-
?
6.3.2.6 additional information in lower organisms PurC and PurE are not fused as in higher organisms, active site structure, overview Saccharomyces cerevisiae ?
-
?

Subunits

EC Number Subunits Comment Organism
6.3.2.6 dimer structure overview Thermotoga maritima
6.3.2.6 dimer structure overview, PDB ID 2GQS Escherichia coli
6.3.2.6 monomer structure overview Saccharomyces cerevisiae
6.3.2.6 octamer 4 dimers of PurC around a core of octameric PurE, the PurC dimers do not contact each other, structure overview, PDB ID 2H31 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
6.3.2.6 More the enzyme is a member of the ATP-grasp superfamily Escherichia coli
6.3.2.6 More the enzyme is a member of the ATP-grasp superfamily Homo sapiens
6.3.2.6 More the enzyme is a member of the ATP-grasp superfamily Thermotoga maritima
6.3.2.6 More the enzyme is a member of the ATP-grasp superfamily Saccharomyces cerevisiae
6.3.2.6 PurC
-
Escherichia coli
6.3.2.6 PurC
-
Thermotoga maritima
6.3.2.6 PurC
-
Saccharomyces cerevisiae
6.3.2.6 PurCE
-
Homo sapiens
6.3.2.6 SAICAR synthase
-
Escherichia coli
6.3.2.6 SAICAR synthase
-
Homo sapiens
6.3.2.6 SAICAR synthase
-
Thermotoga maritima
6.3.2.6 SAICAR synthase
-
Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.6 ATP
-
Escherichia coli
6.3.2.6 ATP
-
Homo sapiens
6.3.2.6 ATP
-
Thermotoga maritima
6.3.2.6 ATP
-
Saccharomyces cerevisiae