Amidophosphoribosyltransferase
Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme that in humans is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene.[1][2]
Function
ATase is an enzyme that converts α-phosphoribosylpyrophosphate (α-PRPP) into 5-β-phosphoribosylamine. The enzyme uses the ammonia group from the glutamine side-chain. This is the committing step in de novo purine synthesis. It is allosterically inhibited by AMP, GMP, and IMP.
ATase is a member of the purine/pyrimidine phosphoribosyltransferase family. This protein is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis.[1]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective Wikipedia articles. [3]
Fluorouracil (5-FU) Activity
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References
Further reading
- Iwahana H, Oka J, Mizusawa N, et al. (1993). "Molecular cloning of human amidophosphoribosyltransferase.". Biochem. Biophys. Res. Commun. 190 (1): 192–200. doi:10.1006/bbrc.1993.1030. PMID 8380692.
- Gassmann MG, Stanzel A, Werner S (1999). "Growth factor-regulated expression of enzymes involved in nucleotide biosynthesis: a novel mechanism of growth factor action.". Oncogene 18 (48): 6667–76. doi:10.1038/sj.onc.1203120. PMID 10597272.
- Chen S, Nagy PL, Zalkin H (1997). "Role of NRF-1 in bidirectional transcription of the human GPAT-AIRC purine biosynthesis locus.". Nucleic Acids Res. 25 (9): 1809–16. doi:10.1093/nar/25.9.1809. PMC 146651. PMID 9108165. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=146651.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Stanley W, Chu EH (1978). "Assignment of the gene for phosphoribosylpyrophosphate amidotransferase to the pter leads to q21 region of human chromosome 4.". Cytogenet. Cell Genet. 22 (1-6): 228–31. doi:10.1159/000130943. PMID 752480.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Bera AK, Chen S, Smith JL, Zalkin H (1999). "Interdomain signaling in glutamine phosphoribosylpyrophosphate amidotransferase.". J. Biol. Chem. 274 (51): 36498–504. doi:10.1074/jbc.274.51.36498. PMID 10593947.
- Zalkin H, Dixon JE (1992). "De novo purine nucleotide biosynthesis.". Prog. Nucleic Acid Res. Mol. Biol. 42: 259–87. PMID 1574589.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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2.4.1: Hexosyl-
transferases |
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B3GAT1, B3GAT2, B3GAT3
UGT1A1, UGT1A3, UGT1A4, UGT1A5, UGT1A6, UGT1A7, UGT1A8, UGT1A9, UGT1A10
UGT2A1, UGT2A2, UGT2A3, UGT2B4, UGT2B7, UGT2B10, UGT2B11, UGT2B15, UGT2B17, UGT2B28
Hyaluronan synthase: HAS1 · HAS2 · HAS3
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2.4.2: Pentosyl-
transferases |
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2.4.99: Sialyl
transferases |
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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| Purine metabolism |
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| Pyrimidine metabolism |
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| Deoxyribonucleotides |
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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