Agmatinase

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 PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
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 ${\displaystyle \rightleftharpoons }$ 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

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 15,571,699 bp [1] End 15,585,051 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D3 Start 141,473,983 bp [2] End 141,486,574 bp [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 the AGMAT gene. ^{[5] [6] [7] [8]}

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. GRCh38: Ensembl release 89: ENSG00000116771 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040706 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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. S2CID   31927397.
7. 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.
8. "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. 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 .