Agmatinase

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agmatinase
1woi.jpg
agmatinase hexamer, Deinococcus radiodurans
Identifiers
EC number3.5.3.11
CAS number37289-16-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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

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
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for AGMAT
Genomic location for AGMAT
Band1p36.21Start15,571,699 bp[1]
End15,585,051 bp[1]
RNA expression pattern
PBB GE AGMAT 221648 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_024758

NM_001081408

RefSeq (protein)

NP_079034

NP_001074877

Location (UCSC)Chr 1: 15.57 – 15.59 MbChr 4: 141.75 – 141.76 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]

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.
  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)".

External links[edit]