Arginase

Arginase
Ribbon diagram of human arginase I trimer. PDB entry 2pha[1]
Identifiers
EC no.3.5.3.1
CAS no.9000-96-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Liver arginase
Identifiers
SymbolARG1
NCBI gene383
HGNC663
OMIM608313
RefSeqNM_000045
UniProtP05089
Other data
EC number3.5.3.1
LocusChr. 6 q23
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StructuresSwiss-model
DomainsInterPro
Arginase, type II
Identifiers
SymbolARG2
NCBI gene384
HGNC664
OMIM107830
RefSeqNM_001172
UniProtP78540
Other data
EC number3.5.3.1
LocusChr. 14 q24.1
Search for
StructuresSwiss-model
DomainsInterPro

Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:

arginine + H2Oornithine + urea

It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life.

  1. ^ Di Costanzo L, Pique ME, Christianson DW (May 2007). "Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster". J. Am. Chem. Soc. 129 (20): 6388–9. doi:10.1021/ja071567j. PMC 2593847. PMID 17469833.