Agmatinase

agmatinase
Identifiers
EC number	3.5.3.11
CAS number	37289-16-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction

agmatine + H₂O $\rightleftharpoons$ 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, and SpeB. This enzyme participates in urea cycle and metabolism of amino groups.

Genetics

Agmatine ureohydrolase (agmatinase)
Identifiers
Symbols	AGMAT ; FLJ23384
External IDs	MGI: 1923236 HomoloGene: 99855 GeneCards: AGMAT Gene
EC number	3.5.3.11
Gene ontology Molecular function • agmatinase activity • metal ion binding Cellular component • mitochondrion • extracellular exosome Biological process • polyamine metabolic process • spermidine biosynthetic process • putrescine biosynthetic process from arginine • cellular nitrogen compound metabolic process • small molecule metabolic process • agmatine biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	79814	75986
Ensembl	ENSG00000116771	ENSMUSG00000040706
UniProt	Q9BSE5	A2AS89
RefSeq (mRNA)	NM_024758	NM_001081408
RefSeq (protein)	NP_079034	NP_001074877
Location (UCSC)	Chr 1: 15.57 – 15.59 Mb	Chr 4: 141.75 – 141.76 Mb
PubMed search

In humans, the enzyme is encoded by the AGMAT gene.^[1][2][3][4]

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

1. Mistry SK, Burwell TJ, Chambers RM, Rudolph-Owen L, Spaltmann F, Cook WJ, Morris SM Jr (Jan 2002). "Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus". Am J Physiol Gastrointest Liver Physiol 282 (2): G375–81. doi:10.1152/ajpgi.00386.2001. PMID 11804860.
2. Dallmann K, Junker H, Balabanov S, Zimmermann U, Giebel J, Walther R (Dec 2003). "Human agmatinase is diminished in the clear cell type of renal cell carcinoma". Int J Cancer 108 (3): 342–7. doi:10.1002/ijc.11459. PMID 14648699.
3. Iyer RK, Kim HK, Tsoa RW, Grody WW, Cederbaum SD (Mar 2002). "Cloning and characterization of human agmatinase". Mol Genet Metab 75 (3): 209–18. doi:10.1006/mgme.2001.3277. PMID 11914032.
4. "Entrez Gene: AGMAT agmatine ureohydrolase (agmatinase)".

• 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.
• 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. 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 Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 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. 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. PMC 250384. PMID 4908780.
• Vicente C and 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 US National Library of Medicine Medical Subject Headings (MeSH)