Agmatinase: Difference between revisions

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*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Kim KH, Ahn HJ, Kim DJ |title=Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase |journal=Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |volume=61 |issue= Pt 10 |pages= 889–91 |year= 2006 |pmid= 16511187 |doi= 10.1107/S1744309105027193  | pmc=1991308 |display-authors=etal}}
*{{cite journal  | vauthors=Kim KH, Ahn HJ, Kim DJ |title=Expression, crystallization and preliminary X-ray crystallographic analysis of human agmatinase |journal=Acta Crystallographica Section F |volume=61 |issue= Pt 10 |pages= 889–91 |year= 2006 |pmid= 16511187 |doi= 10.1107/S1744309105027193  | pmc=1991308 |display-authors=etal}}
*{{cite journal  | vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |display-authors=etal}}
*{{cite journal  | vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |display-authors=etal}}
* {{cite journal | vauthors = Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK | date = 1970 | title = Isolation and Characterization of a Mutant of Escherichia coli Blocked in the Synthesis of Putrescine | journal = J. Bacteriol. | volume = 101 | pages = 725–30  | pmid = 4908780 | issue = 3 | pmc = 250384 }}
* {{cite journal | vauthors = Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK | date = 1970 | title = Isolation and Characterization of a Mutant of Escherichia coli Blocked in the Synthesis of Putrescine | journal = J. Bacteriol. | volume = 101 | pages = 725–30  | pmid = 4908780 | issue = 3 | pmc = 250384 }}

Latest revision as of 15:32, 8 October 2018

agmatinase
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 <math>\rightleftharpoons</math> 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

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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)".

External links