BREAKING NEWS
Cloud Server Hosting For Online Businesses
Inexpensive SEO Services
Benefits of Wanting to play Free Online Slot machines
Agmatinase

Summary

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

agmatinase
agmatinase hexamer, Deinococcus radiodurans
Identifiers
EC no.3.5.3.11
CAS no.37289-16-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
agmatine + H2O 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 edit

AGMAT
Identifiers
AliasesAGMAT, Agmatinase
External IDsOMIM: 617887 MGI: 1923236 HomoloGene: 99855 GeneCards: AGMAT
Orthologs
SpeciesHumanMouse
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 MbChr 4: 141.47 – 141.49 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

In humans, the enzyme is encoded by the AGMAT gene.[5][6][7][8]

Structural studies edit

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 edit

  • Piperazine-1-carboxamidine

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116771 – Ensembl, May 2017
  2. ^ a b c 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 edit