ARG1

Identifiers

Aliases

External IDs

GeneCards:

Orthologs

Species

Human

Mouse

Entrez


n/a


n/a

Ensembl


n/a


n/a

UniProt


n/a


n/a

RefSeq (mRNA)


n/a


n/a

RefSeq (protein)


n/a


n/a

Location (UCSC)

n/a

PubMed search

n/a

Wikidata

View/Edit Human

Arginase, liver is an enzyme that in humans is encoded by the ARG1 gene.^[1]

References

↑ "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

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)

This article is issued from Wikipedia - version of the 5/19/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

ARG1

References

Further reading