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