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Literature summary for 2.1.2.3 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene purH
-

Purification (Commentary)

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

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
N10-formyltetrahydrofolate
-
Escherichia coli

General Information

General Information Comment Organism
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