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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.21 protein sequence is used in model building on Trchoderma ni enzyme crystals providing an excellent fit to the electron density. Comparison to the structure of human enzyme Bombyx mori
4.1.1.21 to 2.8 A resolution, space-group P22121 with one homo-tetramer in the asymmetric unit. Comparison to the structure of human enzyme Trichoplusia ni
6.3.2.6 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.21 50000
-
 8 * 50000, SDS-PAGE Trichoplusia ni
4.1.1.21 360000
-
 gel filtration Trichoplusia ni
6.3.2.6 50000
-
 x * 50000, SDS-PAGE Trichoplusia ni
6.3.2.6 360000
-
 gel filtration Trichoplusia ni

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 Trichoplusia ni
-
 ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.21 Bombyx mori Q1HQ66
-
-
4.1.1.21 Trichoplusia ni
-
-
-
6.3.2.6 Trichoplusia ni
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.21
-
 Trichoplusia ni
6.3.2.6 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)

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
-
 Trichoplusia ni ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.21 octamer 8 * 50000, SDS-PAGE Trichoplusia ni
6.3.2.6 More structure modeling, overview Trichoplusia ni
6.3.2.6 oligomer x * 50000, SDS-PAGE Trichoplusia ni

Synonyms

EC Number Synonyms Comment Organism
6.3.2.6 4-(N-succinylcarboxamide)-5-aminoimidazole ribonucleotide synthetase
-
 Trichoplusia ni
6.3.2.6 PAICS
-
 Trichoplusia ni
6.3.2.6 SAICAR synthase
-
 Trichoplusia ni

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.6 ATP
-
 Trichoplusia ni

General Information

EC Number General Information Comment Organism
6.3.2.6 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