Comments: |
Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme requires ATP and utilizes formate, which is provided by the hydrolysis of 10-formyltetrahydrofolate by EC 3.5.1.10, formyltetrahydrofolate deformylase. The other enzyme, EC 2.1.2.2, phosphoribosylglycinamide formyltransferase 1, utilizes 10-formyltetrahydrofolate directly. Formyl phosphate is formed during catalysis as an intermediate. The enzyme from the bacterium Escherichia coli can also catalyse the activity of EC 2.7.2.1, acetate kinase. |
References: |
1. |
Nagy, P.L., McCorkle, G.M. and Zalkin, H. purU, a source of formate for purT-dependent phosphoribosyl-N-formylglycinamide synthesis. J. Bacteriol. 175 (1993) 7066–7073. [DOI] [PMID: 8226647] |
2. |
Nygaard, P. and Smith, J.M. Evidence for a novel glycinamide ribonucleotide transformylase in Escherichia coli. J. Bacteriol. 175 (1993) 3591–3597. [DOI] [PMID: 8501063] |
3. |
Marolewski, A., Smith, J.M. and Benkovic, S.J. Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli. Biochemistry 33 (1994) 2531–2537. [DOI] [PMID: 8117714] |
4. |
Marolewski, A.E., Mattia, K.M., Warren, M.S. and Benkovic, S.J. Formyl phosphate: a proposed intermediate in the reaction catalyzed by Escherichia coli PurT GAR transformylase. Biochemistry 36 (1997) 6709–6716. [DOI] [PMID: 9184151] |
5. |
Thoden, J.B., Firestine, S., Nixon, A., Benkovic, S.J. and Holden, H.M. Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase. Biochemistry 39 (2000) 8791–8802. [DOI] [PMID: 10913290] |
6. |
Jelsbak, L., Mortensen, M.IB., Kilstrup, M. and Olsen, J.E. The in vitro redundant enzymes PurN and PurT are both essential for systemic infection of mice in Salmonella enterica serovar Typhimurium. Infect. Immun. 84 (2016) 2076–2085. [DOI] [PMID: 27113361] |
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