agmatinase
agmatinase hexamer, Deinococcus radiodurans
Identifiers
EC no.	3.5.3.11
CAS no.	37289-16-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDBPDBePDBsum
Gene Ontology	AmiGO /QuickGO
Search PMC articles PubMed articles NCBI proteins

Inenzymology, anagmatinase (EC3.5.3.11) is anenzyme thatcatalyzes thechemical reaction

agmatine + H₂O${\displaystyle \rightleftharpoons }$putrescine +urea

Thus, the twosubstrates of this enzyme areagmatine andH₂O, whereas its twoproducts areputrescine andurea.

This enzyme belongs to the family ofhydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Thesystematic name of this enzyme class isagmatine amidinohydrolase. Other names in common use includeagmatine ureohydrolase. This enzyme participates inurea cycle and metabolism of amino groups.

AGMAT
Identifiers
Aliases	AGMAT, Agmatinase
External IDs	OMIM:617887;MGI:1923236;HomoloGene:99855;GeneCards:AGMAT;OMA:AGMAT - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.21 Start 15,571,699bp[1] End 15,585,051bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D3 Start 141,473,983bp[2] End 141,486,574bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in glomerulus kidney tubule metanephric glomerulus renal medulla buccal mucosa cell human kidney jejunal mucosa liver vastus lateralis muscle mucosa of colon Top expressed in left lobe of liver epithelium of small intestine motor neuron duodenum Paneth cell fetal liver hematopoietic progenitor cell jejunum habenula migratory enteric neural crest cell morula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines hydrolase activity metal ion binding agmatinase activity Cellular component mitochondrion Biological process putrescine biosynthetic process agmatine biosynthetic process spermidine biosynthetic process putrescine biosynthetic process from arginine Sources:Amigo /QuickGO
Orthologs Species Human Mouse Entrez 79814 75986 Ensembl ENSG00000116771 ENSMUSG00000040706 UniProt Q9BSE5 A2AS89 RefSeq (mRNA) NM_024758 NM_001081408 NM_001378862 RefSeq (protein) NP_079034 NP_001074877 NP_001365791 Location (UCSC) Chr 1: 15.57 – 15.59 Mb Chr 4: 141.47 – 141.49 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

In humans, the enzyme is encoded by theAGMATgene.^[5][6][7][8]

As of late 2007, 5structures have been solved for this class of enzymes, withPDB accession codes1GQ6,1GQ7,1WOG,1WOH, and1WOI.

• Piperazine-1-carboxamidine

• 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 MedicineMedical Subject Headings (MeSH)

• HumanAGMAT genome location andAGMAT gene details page in theUCSC Genome Browser.

• Genes on human chromosome 1
• EC 3.5.3
• Enzymes of known structure
• EC 3.5 stubs

• Articles with short description
• Short description matches Wikidata
• All stub articles