ARG1

Arginase 1

Crystal structure of human arginase I trimer. PDB entry 2pha ^[1]

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WVA, 1WVB, 2AEB, 2PHA, 2PHO, 2PLL, 2ZAV, 3DJ8, 3E6K, 3E6V, 3F80, 3GMZ, 3GN0, 3KV2, 3LP4, 3LP7, 3MFV, 3MFW, 3MJL, 3SJT, 3SKK, 3TF3, 3TH7, 3THE, 3THH, 3THJ, 4FCI, 4FCK, 4GSM, 4GSV, 4GSZ, 4GWC, 4GWD, 4HWW, 4HXQ, 4IE1

Identifiers

Symbol

ARG1

External IDs

OMIM: 608313 HomoloGene: 29 GeneCards: ARG1 Gene

EC number

3.5.3.1

Gene ontology
Molecular function	• arginase activity • manganese ion binding
Cellular component	• extracellular space • nucleus • cytoplasm • mitochondrial outer membrane • cytosol • neuron projection • neuronal cell body • extracellular exosome
Biological process	• urea cycle • liver development • positive regulation of endothelial cell proliferation • arginine catabolic process • aging • response to herbicide • response to manganese ion • response to zinc ion • response to selenium ion • regulation of L-arginine import • response to amine • arginine catabolic process to ornithine • lung development • collagen biosynthetic process • response to vitamin A • response to vitamin E • cellular nitrogen compound metabolic process • response to drug • response to amino acid • small molecule metabolic process • response to cadmium ion • response to axon injury • response to methylmercury • mammary gland involution • maternal process involved in female pregnancy • protein homotrimerization • cellular response to hydrogen peroxide • cellular response to lipopolysaccharide • cellular response to interleukin-4 • cellular response to glucagon stimulus • cellular response to dexamethasone stimulus • cellular response to transforming growth factor beta stimulus
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

383

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
131.57 – 131.58 Mb

Chr 10:
24.92 – 24.93 Mb

PubMed search

Arginase, liver is an enzyme that in humans is encoded by the ARG1 gene.^[2]

References

↑ Di Costanzo, L.; Pique, M. E.; Christianson, D. W. (2007). "Crystal Structure of Human Arginase I Complexed with Thiosemicarbazide Reveals an Unusual Thiocarbonyl μ-Sulfide Ligand in the Binuclear Manganese Cluster". Journal of the American Chemical Society 129 (20): 6388–6389. doi:10.1021/ja071567j. PMC 2593847. PMID 17469833.
↑ "Entrez Gene: Arginase, liver".

Morris, C. R.; Kato, G. J.; Poljakovic, M.; Wang, X.; Blackwelder, W. C.; Sachdev, V.; Hazen, S. L.; Vichinsky, E. P.; Morris Jr, S. M.; Gladwin, M. T. (2005). "Dysregulated Arginine Metabolism, Hemolysis-Associated Pulmonary Hypertension, and Mortality in Sickle Cell Disease". JAMA 294 (1): 81–90. doi:10.1001/jama.294.1.81. PMC 2065861. PMID 15998894.
Jiang, M.; Ding, Y.; Su, Y.; Hu, X.; Li, J.; Zhang, Z. (2006). "Arginase-flotillin interaction brings arginase to red blood cell membrane". FEBS Letters 580 (28–29): 6561–6564. doi:10.1016/j.febslet.2006.11.003. PMID 17113085.
Morris Jr, S. M. (2009). "Recent advances in arginine metabolism: Roles and regulation of the arginases". British Journal of Pharmacology 157 (6): 922–930. doi:10.1111/j.1476-5381.2009.00278.x. PMC 2737650. PMID 19508396.
Rotondo, R.; Bertolotto, M.; Barisione, G.; Astigiano, S.; Mandruzzato, S.; Ottonello, L.; Dallegri, F.; Bronte, V.; Ferrini, S.; Barbieri, O. (2011). "Exocytosis of azurophil and arginase 1-containing granules by activated polymorphonuclear neutrophils is required to inhibit T lymphocyte proliferation". Journal of Leukocyte Biology 89 (5): 721–727. doi:10.1189/jlb.1109737. PMID 21330347.
Shapiro, M. B.; Senapathy, P. (1987). "RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression". Nucleic Acids Research 15 (17): 7155–7174. doi:10.1093/nar/15.17.7155. PMC 306199. PMID 3658675.
Rotondo, R.; Barisione, G.; Mastracci, L.; Grossi, F.; Orengo, A. M.; Costa, R.; Truini, M.; Fabbi, M.; Ferrini, S.; Barbieri, O. (2009). "IL-8 induces exocytosis of arginase 1 by neutrophil polymorphonuclears in nonsmall cell lung cancer". International Journal of Cancer 125 (4): 887–893. doi:10.1002/ijc.24448. PMID 19431148.
Salam, M. T.; Bastain, T. M.; Rappaport, E. B.; Islam, T.; Berhane, K.; Gauderman, W. J.; Gilliland, F. D. (2011). "Genetic variations in nitric oxide synthase and arginase influence exhaled nitric oxide levels in children". Allergy 66 (3): 412–419. doi:10.1111/j.1398-9995.2010.02492.x. PMC 3058253. PMID 21039601.
Gannon, P. O.; Godin-Ethier, J.; Hassler, M.; Delvoye, N.; Aversa, M.; Poisson, A. O.; Péant, B.; Alam Fahmy, M.; Saad, F.; Lapointe, R. J.; Mes-Masson, A. M. (2010). Creighton, Chad, ed. "Androgen-Regulated Expression of Arginase 1, Arginase 2 and Interleukin-8 in Human Prostate Cancer". PLoS ONE 5 (8): e12107. doi:10.1371/journal.pone.0012107. PMC 2920336. PMID 20711410.
Ishikawa, T.; Harada, T.; Koi, H.; Kubota, T.; Azuma, H.; Aso, T. (2007). "Identification of Arginase in Human Placental Villi". Placenta 28 (2–3): 133–138. doi:10.1016/j.placenta.2006.03.015. PMID 16720041.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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ARG1

References

Further reading