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InterPro: IPR005924 Arginase

Protein matches Help

UniProtKB

Matches:

1295 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR005924 Arginase

Secondary

IPR000287

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00116	ARGINASE	1295
Signatures in BioMart

InterPro Relationships Help

Parent

IPR006035 Ureohydrolase

Children

IPR014033 Arginase, subgroup

Contains

IPR020855 Ureohydrolase, manganese-binding site

GO Term annotation Help

Function

GO:0016787 hydrolase activity
GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

L-Arginine is converted to nitric oxide and citrulline by the enzyme nitric oxide synthase and by the enzyme arginase as a part of the hepatic urea cycle. Arginase is a manganese metalloenzymes containing a metal-activated hydroxide ion, a critical nucleophile in metalloenzymes that catalyze hydrolysis or hydration reactions. A hydrogen bond formed by the metal-bound hydroxide holds the enzyme in the proper orientation for catalysis however nonmetal substrate-binding sites are also implicated in the enzyme mechanism. Regeneration of metal-bound hydroxide ion from a metal-bound water molecule requires proton transfer to bulk solvent mediated by a histidine proton shuttle residue.

Structural links Help

PDB - click here

SCOP: c.42.1.1

CATH: 3.40.800.10

Database links Help

Enzyme: EC:3.5.3

Blocks: IPB005924

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005924

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2AS89 Agmatinase, mitochondrial

P00812 Arginase

P05089 Arginase-1

P37819 Proclavaminate amidinohydrolase

P73270 Probable agmatinase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014033	Arginase, subgroup
IPR006035	Ureohydrolase
IPR020855	Ureohydrolase, manganese-binding site
IPR005924	Arginase
IPR005925	Putative agmatinase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Haraguchi Y, Takiguchi M, Amaya Y, Kawamoto S, Matsuda I, Mori M. Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc. Natl. Acad. Sci. U.S.A. 84 1987 412-5 [PubMed: 3540966] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=3540966
	Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW. Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. Proc. Natl. Acad. Sci. U.S.A. 102 2005 13058-63 [PubMed: 16141327] http://dx.doi.org/10.1073/pnas.0504027102
	Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE. Probing the role of the hyper-reactive histidine residue of arginase. Arch. Biochem. Biophys. 444 2005 15-26 [PubMed: 16266687] http://dx.doi.org/10.1016/j.abb.2005.09.009
	Sumrada RA, Cooper TG. Nucleotide sequence of the Saccharomyces cerevisiae arginase gene (CAR1) and its transcription under various physiological conditions. J. Bacteriol. 160 1984 1078-87 [PubMed: 6094498] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=6094498
	Xu Q, Baker BS, Tata JR. Developmental and hormonal regulation of the Xenopus liver-type arginase gene. Eur. J. Biochem. 211 1993 891-8 [PubMed: 7916684] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17622.x
	Di Costanzo L, Pique ME, Christianson DW. 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 2007 6388-9 [PubMed: 17469833] http://dx.doi.org/10.1021/ja071567j
	Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW. Expression, purification, assay, and crystal structure of perdeuterated human arginase I. Arch. Biochem. Biophys. 465 2007 82-9 [PubMed: 17562323] http://dx.doi.org/10.1016/j.abb.2007.04.036
	Zakharian TY, Di Costanzo L, Christianson DW. Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I. Org. Biomol. Chem. 6 2008 3240-3 [PubMed: 18802628] http://dx.doi.org/10.1039/b811797g

InterPro 23.1