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Literature summary for 6.3.2.6 extracted from

  • Taschner, M.; Basquin, J.; Benda, C.; Lorentzen, E.
    Crystal structure of the invertebrate bifunctional purine biosynthesis enzyme PAICS at 2.8 A resolution (2013), Proteins, 81, 1473-1478.
    View publication on PubMed
Search for more literature for 6.3.2.6

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme in insect HighFive cells Trichoplusia ni

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Trichoplusia ni

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 x * 50000, SDS-PAGE Trichoplusia ni
360000
-
 gel filtration Trichoplusia ni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate Trichoplusia ni
-
 ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
 ?

Organism

Organism UniProt Comment Textmining
Trichoplusia ni
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from insect HighFive cells by nickel affinity and anion exchange chromatography, followed by gel filtration Trichoplusia ni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate
-
 Trichoplusia ni ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
 ?

Subunits

Subunits Comment Organism
More structure modeling, overview Trichoplusia ni
oligomer x * 50000, SDS-PAGE Trichoplusia ni

Synonyms

Synonyms Comment Organism
4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase
-
 Trichoplusia ni
PAICS
-
 Trichoplusia ni
SAICAR synthase
-
 Trichoplusia ni

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Trichoplusia ni

General Information

General Information Comment Organism
additional information 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 Trichoplusia ni