- Source: Agmatinase
In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction
agmatine + H2O
⇌
{\displaystyle \rightleftharpoons }
putrescine + urea
Thus, the two substrates of this enzyme are agmatine and H2O, whereas its two products are putrescine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is agmatine amidinohydrolase. Other names in common use include agmatine ureohydrolase. This enzyme participates in urea cycle and metabolism of amino groups.
Genetics
In humans, the enzyme is encoded by the AGMAT gene.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GQ6, 1GQ7, 1WOG, 1WOH, and 1WOI.
Inhibitors
Piperazine-1-carboxamidine
References
Morris SM (2004). "Vertebrate agmatinases: what role do they play in agmatine catabolism?". Ann. N. Y. Acad. Sci. 1009: 30–3. doi:10.1196/annals.1304.003. PMID 15028567. S2CID 24146429.
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.
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.
Chen FW, Davies JP, Ioannou YA (1998). "Differential gene expression in apoptosis: identification of ribosomal protein 23K, a cell proliferation inhibitor". Mol. Genet. Metab. 64 (4): 271–82. doi:10.1006/mgme.1998.2718. PMID 9758718.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Kim KH, Ahn HJ, Kim DJ, et al. (2006). "Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase". Acta Crystallographica Section F. 61 (Pt 10): 889–91. doi:10.1107/S1744309105027193. PMC 1991308. PMID 16511187.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK (1970). "Isolation and Characterization of a Mutant of Escherichia coli Blocked in the Synthesis of Putrescine". J. Bacteriol. 101 (3): 725–30. doi:10.1128/JB.101.3.725-730.1970. PMC 250384. PMID 4908780.
Vicente C, Legaz ME (1982). "Preparation and properties of agmatine amidinohydrolase of Evernia prunastri". Physiol. Plant. 55: 335–339. doi:10.1111/j.1399-3054.1982.tb00301.x.
agmatinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
External links
Human AGMAT genome location and AGMAT gene details page in the UCSC Genome Browser.
