Phosphoribosylaminoimidazole carboxylase
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<StructureSection load='' size='350' side='right' caption='Structure of E. coli PurE octamer complex with 5-aminoimidazole ribonucleotide (AIR) (PDB entry [[1d7a]])' scene='57/571253/Cv/1'> | <StructureSection load='' size='350' side='right' caption='Structure of E. coli PurE octamer complex with 5-aminoimidazole ribonucleotide (AIR) (PDB entry [[1d7a]])' scene='57/571253/Cv/1'> | ||
== Function == | == Function == | ||
| - | '''Phosphoribosylaminoimidazole carboxylase (PurE)''' is part of the purine biosynthesis and | + | '''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<ref>PMID:1534690</ref>. '''PurK''' catalyzes the conversion of AIR,ATP and bicarbonate to N5-CAIR, ADP and phosphate. |
== Structural highlights == | == Structural highlights == | ||
Current revision
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References
- ↑ 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
- ↑ 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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