Phosphoribosylaminoimidazole carboxylase

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Function

Phosphoribosylaminoimidazole carboxylase (PurE) or N5-carboxyaminoimidazole ribonucleotide mutase is part of the purine biosynthesis and catalyzes the reversible conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 5-aminoimidazole ribonucleotide (AIR). In bacteria PurE and PurK or Phosphoribosylaminoimidazole carboxylase ATPase subunit are independent enzymes while in plants and fungi it is a domain of phosphoribosylaminoimidazole carboxylase[1]. PurK catalyzes the conversion of AIR,ATP and bicarbonate to N5-CAIR, ADP and phosphate.

Structural highlights

The biological assembly of E. coli PurE is . PurE is located in a [2]. Water molecule is shown as red sphere.

3D structures of PurE

Phosphoribosylaminoimidazole carboxylase 3D structures


Structure of E. coli PurE octamer complex with 5-aminoimidazole ribonucleotide (AIR) (PDB entry 1d7a)

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ReferencesReferences

  1. Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM. Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway. Biochemistry. 1992 Jun 2;31(21):5022-32. PMID:1534690
  2. Mathews II, Kappock TJ, Stubbe J, Ealick SE. Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway. Structure. 1999 Nov 15;7(11):1395-406. PMID:10574791

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