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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
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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
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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
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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
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metabolism
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4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase (PurC) is a key enzyme in the de novo purine biosynthetic pathway of bacteria
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metabolism
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the enzyme is involved in the purine nucleotide metabolism, catalyzing the formation pf a pecursor of cordycepin
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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 condiÂtion. 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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