Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Qiu, X.; Yuan, Y.; Gao, Y.
    Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli (2011), Acta Crystallogr. Sect. F, 67, 1590-1594.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.3 gene purH, expression of N-terminally His6-tagged PurH in Escherichia coli strain Rosetta (DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.3 purified recombinant His6-tagged PurH, without methylation of the 28 lysine residues, sitting drop vapour diffusion method, mixing of 0.001 ml of 56 mg/ml protein in 0.8 M sodium/potassium hydrogen phosphate, pH 7.5, with 0.001 ml of reservoir solution containing 0.1 M sodium acetate, pH 5.0, 1 M ammonium sulfate, 1 week to 1 month, X-ray diffraction structure determination and analysis at 3.05 A resolution Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.3 additional information specific antifolate reagents and nonfolate inhibitors are analogues of cofactor N10-formyltetrahydrofolate and can completely inhibit AICAR Tfase activity Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.3 Escherichia coli
-
 gene purH
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.3 recombinant N-terminally His6-tagged PurH from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration Escherichia coli

Subunits

EC Number Subunits Comment Organism
2.1.2.3 More PurH is composed of two domains linked by a flexible region. The N-terminal domain possesses IMPCH activity and the C-terminal domain possesses AICAR Tfase activity Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.1.2.3 AICAR TFase
-
 Escherichia coli
2.1.2.3 AICAR transformylase
-
 Escherichia coli
2.1.2.3 aminoimidazole-4-carboxamide ribonucleotide transformylase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.3 N10-formyltetrahydrofolate
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.2.3 additional information the enzyme is located at the C-terminus of the bifunctional purine-biosynthesis protein, PurH, whose N-terminus possesses IMP cyclohydrolase activity. Coupling of the two domains is essential for the catalytic process, as the AICAR Tfase reaction favours the reverse direction by itself and the irreversible cyclization of 5-formyl-aminoimidazole-4-carboxamide ribonucleotide to IMP drives formyl transfer in the forward direction Escherichia coli