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Gene Review:

purN - phosphoribosylglycinamide formyltransferase 1

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2496, JW2485, ade

Smith, J.M. et al., Nixon, A.E. et al., Cook, R.J. et al., Almassy, R.J. et al., Inglese, J. et al., et al.

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Disease relevance of purN

5'-Phosphoribosylglycinamide transformylase (EC 2.1.2.2), encoded by the purN gene of Escherichia coli, catalyzes the synthesis of 5'-phosphoribosylformylglycinamide from 5'-phosphoribosylglycinamide (GAR) [1].
The NH2-terminal sequence (residues 1-203) is 24-30% identical to phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) from Bacillus subtilis (30%), Escherichia coli (24%), Drosophila melanogaster (24%), and human hepatoma HepG2 (27%) [2].

High impact information on purN

SCRATCHY libraries were created from the glycinamide-ribonucleotide formyltransferase (GART) genes from Escherichia coli (purN) and human (hGART) [3].
The enzymes encoded by the Escherichia coli genes purU and purN, N10-formyltetrahydrofolate hydrolase and glycinamide ribonucleotide (GAR) transformylase, respectively, catalyze similiar yet distinct reactions [4].
The specific activity of two hybrid proteins was within 100- to 1000-fold of the native purN GAR transformylase validating the approach of constructing an enzyme active site from functional parts of others [4].
The three-dimensional structure of phosphoribosylglycinamide formyltransferase (10-formyltetrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2) has been solved both as an apoenzyme at 2.8-A resolution and as a ternary complex with the substrate glycinamide ribonucleotide and a folate inhibitor at 2.5-A resolution [5].
The sequence identity to phosphoribosylglycinamide formyltransferase is discussed, and a binding region for 10-formyltetrahydrofolate is proposed [2].

Chemical compound and disease context of purN

Glycinamide ribonucleotide transformylase (GAR TFase; EC 2.1.2.2) has been purified 70-fold to apparent homogeneity from Escherichia coli harboring an expression vector encoding the purN gene product, GAR TFase [6].

Biological context of purN

Immediately downstream from the purN gene of the purMN operon is a region of dyad symmetry capable of forming a hairpin stem and loop structure characteristic of a rho-independent terminator [1].
The deduced amino acid sequence of the human and avian polyproteins show extensive sequence homologies to the bacterial purD, purM, and purN encoded proteins [7].

Associations of purN with chemical compounds

The purN gene is located adjacent to and immediately downstream from the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole (AIR) synthetase where the initiation codon for GAR transformylase overlaps the termination codon of AIR synthetase [1].
This enzyme differs from the previously known purN encoded enzyme in size, sequence, and substrates; ATP and formate are required as opposed to formyl tetrahydrofolate [8].

Other interactions of purN

Based on polarity studies, the expression of the purN gene originates from the purM control region and thus forms a purMN operon [1].

References

Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12. Smith, J.M., Daum, H.A. J. Biol. Chem. (1987) [Pubmed]
Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase. Cook, R.J., Lloyd, R.S., Wagner, C. J. Biol. Chem. (1991) [Pubmed]
Creating multiple-crossover DNA libraries independent of sequence identity. Lutz, S., Ostermeier, M., Moore, G.L., Maranas, C.D., Benkovic, S.J. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
Assembly of an active enzyme by the linkage of two protein modules. Nixon, A.E., Warren, M.S., Benkovic, S.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. Almassy, R.J., Janson, C.A., Kan, C.C., Hostomska, Z. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase. Inglese, J., Johnson, D.L., Shiau, A., Smith, J.M., Benkovic, S.J. Biochemistry (1990) [Pubmed]
De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Aimi, J., Qiu, H., Williams, J., Zalkin, H., Dixon, J.E. Nucleic Acids Res. (1990) [Pubmed]
Formyl phosphate: a proposed intermediate in the reaction catalyzed by Escherichia coli PurT GAR transformylase. Marolewski, A.E., Mattia, K.M., Warren, M.S., Benkovic, S.J. Biochemistry (1997) [Pubmed]

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