EC Number |
General Information |
Reference |
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6.3.2.6 | metabolism |
4-(N-succino)-5-aminoimidazole-4-carboxamide ribonucleotide synthetase (PurC) is a key enzyme in the de novo purine biosynthetic pathway of bacteria |
-, 746369 |
6.3.2.6 | 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 |
745942 |
6.3.2.6 | metabolism |
SAICAR synthetase (PurC) is involved in de novo purine biosynthesis |
755775 |
6.3.2.6 | metabolism |
the enzyme is involved in the purine nucleotide metabolism, catalyzing the formation pf a pecursor of cordycepin |
-, 746228 |
6.3.2.6 | 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 |
-, 743939 |
6.3.2.6 | more |
analysis of the dimer structure of enzyme SpPurC, PDB ID 4FE2. Structure comparisons of Streptococcus pneumoniae and Bacillus anthracis PurC enzymes, overview |
-, 746369 |
6.3.2.6 | more |
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 |
728777 |
6.3.2.6 | more |
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 |
746369 |
6.3.2.6 | more |
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 |
-, 743939 |
6.3.2.6 | more |
structure-activity molecular dynamics and simulation using the enzyme crystal structure, modeling, overview |
728030 |