Browse history interactively

Page 1

Page 1Revision 1

Page 2

Page 2Revision 2

← Previous editContent deleted Content addedVisualWikitext

Revision as of 13:05, 24 October 2011 editBeetstra (talk | contribs)Edit filter managers, Administrators172,036 edits Script assisted update of identifiers for the Chem/Drugbox validation project (updated: 'ChEMBL', 'KEGG').← Previous edit		Latest revision as of 19:20, 3 December 2024 edit undoFreaky.jpeg (talk | contribs)42 editsmNo edit summary
(511 intermediate revisions by more than 100 users not shown)
Line 1:		Line 1:
			{{short description|Amino acid}}
	{{Merge from|Arginine pyroglutamate|date=April 2010}}
	{{chembox		{{chembox
			| ImageFile = Arginin - Arginine.svg
	| Verifiedfields = changed
			| IUPACNames=Arginine
	| verifiedrevid = 408396611
			| ImageFile_Ref = {{chemboximage|correct|??}}
	| Name = <small>L</small>-Arginine
			| ImageName = Skeletal formula of arginine
	| ImageFileL1 = L-Arginin - L-Arginine.svg
			| ImageCaption = ] of arginine
	| ImageSizeL1 = 200px
			| ImageClass = skin-invert-image
	| ImageFileR1 = L-arginine-3D-hztl.png
			| ImageFileL2 = Arginine-from-xtal-3D-bs-17.png
	| ImageSizeR1 = 120px
			| ImageCaptionL2 = ]
	| IUPACName = (''S'')-2-Amino-5-guanidinopentanoic acid
	| OtherNames = Arginine		| ImageFileR2 = Arginine-from-xtal-3D-sf.png
			| ImageCaptionR2 = ]
	| Section1 = {{Chembox Identifiers
			| OtherNames = 2-Amino-5-guanidinopentanoic acid
	| UNII_Ref = {{fdacite|correct|FDA}}
			|Section1={{Chembox Identifiers
	| UNII = 94ZLA3W45F
			| index1_label = D/L
	| ChEMBL_Ref = {{ebicite|changed|EBI}}
	| ChEMBL = 179653		| index2_label = D
			| index_label = L <!-- needs to be L arginine (natural isomer) so drugbank etc. take correct index_label -->
	| InChI = 1/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)
			| index3_label = L HCl
	| InChIKey = ODKSFYDXXFIFQN-UHFFFAOYAT
			| CASNo1 = 7200-25-1
	| SMILES1 = C(CC(C(=O)O)N)CNC(=N)N
	| StdInChI_Ref = {{stdinchicite|correct|chemspider}}		| CASNo1_Ref = {{cascite|correct|CAS}}
			| CASNo2 = 157-06-2
	| StdInChI = 1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)
	| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}		| CASNo2_Ref = {{cascite|correct|CAS}}
	| StdInChIKey = ODKSFYDXXFIFQN-UHFFFAOYSA-N
	| CASNo = 74-79-3		| CASNo = 74-79-3
	| CASNo_Ref = {{cascite|correct|CAS}}		| CASNo_Ref = {{cascite|correct|CAS}}
			| CASNo3 = 1119-34-2
	| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
			| CASNo3_Ref = {{cascite|correct|CAS}}
	| ChemSpiderID = 227
			| PubChem1 = 232
			| PubChem2 = 71070
	| PubChem = 6322		| PubChem = 6322
			| ChemSpiderID1 = 227
			| ChemSpiderID1_Ref = {{chemspidercite|correct|chemspider}}
			| ChemSpiderID2 = 64224
			| ChemSpiderID2_Ref = {{chemspidercite|correct|chemspider}}
			| ChemSpiderID = 6082
			| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}
			| UNII1_Ref = {{fdacite|correct|FDA}}
			| UNII2_Ref = {{fdacite|correct|FDA}}
			| UNII_Ref = {{fdacite|correct|FDA}}
			| UNII3_Ref = {{fdacite|correct|FDA}}
			| UNII1 = FL26NTK3EP
			| UNII2 = R54Z304Z7C
			| UNII = 94ZLA3W45F
			| UNII3 = F7LTH1E20Y
			| EINECS = 230-571-3
			| DrugBank = DB00125
			| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
			| KEGG = C02385
	| KEGG_Ref = {{keggcite|correct|kegg}}		| KEGG_Ref = {{keggcite|correct|kegg}}
	| KEGG = D02982		| MeSHName = Arginine
	| IUPHAR_ligand = 721
	| ChEBI_Ref = {{ebicite|changed|EBI}}
	| ChEBI = 29016		| ChEBI = 29016
			| ChEBI_Ref = {{ebicite|correct|EBI}}
	| SMILES = O=C(O)C(N)CCC/N=C(\N)N
			| ChEMBL2 = 212301
			| ChEMBL2_Ref = {{ebicite|correct|EBI}}
			| ChEMBL = 1485
			| ChEMBL_Ref = {{ebicite|correct|EBI}}
			| RTECS = CF1934200 <small>''L''</small>
			| IUPHAR_ligand = 721
			| Beilstein = 1725411, 1725412 <small>''D''</small>, 1725413 <small>''L''</small>
			| Gmelin = 364938 <small>''D''</small>
			| 3DMet = B01331
			| SMILES1 = C(CC(C(=O)O)N)CNC(=N)N
			| Jmol1 = none <!-- needs to be none because Jmol would show L if this SMILES were used -->
			| SMILES = C(C(C(=O)O)N)CNC(=N)N
			| SMILES2 = C(C(C(=O)O)N)CNC(=N)N
			| SMILES3 = .NC(CCCNC(N)=)C()=O
			| SMILES4 = NC(CCCNC(N)=)C()=O
			| SMILES4_Comment = L ]
			| StdInChI = 1S/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/t4-/m0/s1
			| StdInChI_Ref = {{stdinchicite|correct|chemspider}}
			| StdInChIKey = ODKSFYDXXFIFQN-BYPYZUCNSA-N
			| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}
			| InChIKey1 = ODKSFYDXXFIFQN-UHFFFAOYSA-N
			| InChIKey2 = ODKSFYDXXFIFQN-SCSAIBSYSA-N
	}}		}}
	| Section2 = {{Chembox Properties		|Section2={{Chembox Properties
	| C=6 | H=14 | N=4 | O=2		| C=6 | H=14 | N=4 | O=2
	| Appearance =		| Appearance = White crystals
			| Odor = Odourless
	| Density =
	| MeltingPt =		| MeltingPtK = 533
	| BoilingPt =		| BoilingPtC = 368
	| Solubility = }}		| Solubility = 14.87 g/100 mL (20 °C)
			| SolubleOther = slightly soluble in ]<br />insoluble in ]
	| Section3 = {{Chembox Hazards
			| LogP = −1.652
	| MainHazards =
			| pKa = 2.18 (carboxyl), 9.09 (amino), 13.8 (guanidino)
	| FlashPt =
	| Autoignition = }}
			}}
			|Section5={{Chembox Thermochemistry
			| DeltaHf = −624.9–−622.3 kJ mol<sup>−1</sup>
			| DeltaHc = −3.7396–−3.7370 MJ mol<sup>−1</sup>
			| Entropy = 250.6 J K<sup>−1</sup> mol<sup>−1</sup>
			| HeatCapacity = 232.8 J K<sup>−1</sup> mol<sup>−1</sup> (at 23.7 °C)
			}}
			|Section6={{Chembox Pharmacology
			| ATC_Supplemental = {{aTC|B05|XB01}} <small>''S''</small>
			}}
			|Section7={{Chembox Hazards
			| ExternalSDS = {{URL|1=https://www.sigmaaldrich.com/US/en/sds/sigma/11009
			|2=L-Arginine}}
			| GHSPictograms = {{gHS exclamation mark}}
			| GHSSignalWord = '''WARNING'''
			| HPhrases = {{h-phrases|319}}
			| PPhrases = {{p-phrases|305+351+338}}
			| LD50 = 5110 mg/kg (rat, oral)
			}}
			|Section8={{Chembox Related
			| OtherFunction_label = alkanoic acids
			| OtherFunction = {{unbulleted list|]|]|]|]|]}}
			| OtherCompounds = {{unbulleted list|]}}
	}}		}}
			}}
	'''Arginine''' (abbreviated as '''Arg''' or '''R''')<ref>{{cite web | author=IUPAC-IUBMB Joint Commission on Biochemical Nomenclature | title=Nomenclature and Symbolism for Amino Acids and Peptides | work=Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc | url=http://www.chem.qmul.ac.uk/iupac/AminoAcid/ | accessdate=2007-05-17}}</ref> is an α-]. The ] is one of the 20 most common natural amino acids. At the level of molecular genetics, in the structure of the messenger ribonucleic acid ], CGU, CGC, CGA, CGG, AGA, and AGG, are the triplets of nucleotide bases or ] that codify for arginine during protein synthesis. In mammals, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual.<ref name="tapiero">{{cite journal | last = Tapiero | first = H. | coauthors = ''et al.'' | title = L-Arginine | journal = Biomedicine and Pharmacotherapy | volume = 56 | issue = 9 | year = 2002 | month = November | pages = 439–445 REVIEW | pmid = 12481980 | accessdate = 2009-11-29 | doi=10.1161/hc3301.094910}}</ref> Preterm infants are unable to synthesize or create arginine internally, making the amino acid nutritionally essential for them.<ref>{{cite journal | last = Wu | first = G. | coauthors = ''et al.'' | title = Arginine deficiency in preterm infants: biochemical mechanisms and nutritional implications | journal = Journal of Nutritional Biochemistry | volume = 15 | issue = 8 | year = 2004| month = August | pages = 332–451 REVIEW | pmid = 15302078 | accessdate = 2009-11-29 | doi = 10.1016/j.jnutbio.2003.11.010 }}</ref> There are some conditions that put an increased demand on the body for the synthesis of <small>L</small>-arginine, including surgical or other trauma, sepsis and burns.{{Citation needed|date=June 2011}} Arginine was first isolated from a ] seedling extract in 1886 by the Swiss chemist Ernst Schultze.
			'''Arginine''' is the ] with the formula (H<sub>2</sub>N)(HN)CN(H)(CH<sub>2</sub>)<sub>3</sub>CH(NH<sub>2</sub>)CO<sub>2</sub>H. The molecule features a ] group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO<sub>2</sub><sup>−</sup>) and both the amino and guanidino groups are protonated, resulting in a cation. Only the {{sm|l}}-arginine (symbol '''Arg''' or '''R''') enantiomer is found naturally.<ref>{{cite web | url = http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | title = Nomenclature and Symbolism for Amino Acids and Peptides | publisher = IUPAC-IUB Joint Commission on Biochemical Nomenclature | year = 1983 | access-date = 5 March 2018 | archive-url = https://web.archive.org/web/20081009023202/http://www.chem.qmul.ac.uk/iupac/AminoAcid/AA1n2.html | archive-date = 9 October 2008 | url-status = dead }}</ref> Arg residues are common components of ]s. It is ] by the ] CGU, CGC, CGA, CGG, AGA, and AGG.<ref>{{cite web|url=http://www.chem.qmul.ac.uk/iupac/AminoAcid/|title=Nomenclature and Symbolism for Amino Acids and Peptides|author=IUPAC-IUBMB Joint Commission on Biochemical Nomenclature|work=Recommendations on Organic & Biochemical Nomenclature, Symbols & Terminology etc|archive-url=https://web.archive.org/web/20070529233449/http://www.chem.qmul.ac.uk/iupac/AminoAcid/|archive-date=29 May 2007 |url-status=live|access-date=2007-05-17}}</ref> The guanidine group in arginine is the ] for the biosynthesis of ].<ref name=":0">{{Cite book|url=https://books.google.com/books?id=h5FugARr4bgC&pg=PA189|title=Nitric Oxide: Biology and Pathobiology| vauthors = Ignarro LJ |date=2000-09-13|publisher=Academic Press|isbn=978-0-08-052503-7|pages=189|language=en}}</ref> Like all amino acids, it is a white, water-soluble solid.
			The one-letter symbol R was assigned to arginine for its phonetic similarity.<ref name=":02">{{Cite journal |date=10 July 1968 |title=IUPAC-IUB Commission on Biochemical Nomenclature A One-Letter Notation for Amino Acid Sequences |url=https://www.jbc.org/article/S0021-9258(19)34176-6/pdf |journal=Journal of Biological Chemistry |language=en |volume=243 |issue=13 |pages=3557–3559 |doi=10.1016/S0021-9258(19)34176-6|doi-access=free }}</ref>
	In general, most people do not need to take arginine supplements because the body usually produces enough.<ref></ref>
	==Structure==		==History==
			Arginine was first isolated in 1886 from ] seedlings by the German chemist ] and his assistant Ernst Steiger.<ref>{{Cite web|url=http://www.arginium.de/wp-content/uploads/2015/09/Biographie-Ernst-Schulze-Juli-2015.pdf|title=Biographie von Ernst Schulze| vauthors = Apel F |date=July 2015|access-date=2017-11-06 |archive-url=https://web.archive.org/web/20151117031718/http://www.arginium.de/wp-content/uploads/2015/09/Biographie-Ernst-Schulze-Juli-2015.pdf |archive-date=17 November 2015}}</ref><ref>{{cite journal| vauthors = Schulze E, Steiger E |date=1887|title=Ueber das Arginin|trans-title=On arginine|url=https://babel.hathitrust.org/cgi/pt?id=coo.31924078260597;view=1up;seq=55| journal=Zeitschrift für Physiologische Chemie|volume=11|issue=1–2|pages=43–65}}</ref> He named it from the Greek ''árgyros'' (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crystals.<ref>{{cite web |title=BIOETYMOLOGY: ORIGIN IN BIO-MEDICAL TERMS: arginine (Arg R) |url=https://bioetymology.blogspot.com/2012/03/arginin-arg-r.html |access-date=25 July 2019}}</ref> In 1897, Schulze and Ernst Winterstein (1865–1949) determined the structure of arginine.<ref>{{cite journal | vauthors = Schulze E, Winterstein E |title=Ueber ein Spaltungs-product des Arginins |trans-title=On a cleavage product of arginine |language=de |journal=Berichte der Deutschen Chemischen Gesellschaft |date=September 1897 |volume=30 |issue=3 |pages=2879–2882 |doi=10.1002/cber.18970300389 |url=https://zenodo.org/record/1684244 }} The structure for arginine is presented on p. 2882.</ref> Schulze and Winterstein synthesized arginine from ] and ] in 1899,<ref>{{cite journal | vauthors = Schulze E, Winterstein E |title=Ueber die Constitution des Arginins |trans-title=On the constitution of arginine |language=de |journal=Berichte der Deutschen Chemischen Gesellschaft |date=October 1899 |volume=32 |issue=3 |pages=3191–3194 |doi=10.1002/cber.18990320385 |url=https://zenodo.org/record/1617372 }}</ref> but some doubts about arginine's structure lingered<ref>{{cite book | vauthors = Cohen JB |title=Organic Chemistry for Advanced Students, Part 3 |date=1919 |publisher=Longmans, Green & Co. |location=New York, New York, USA |page=140 |edition=2nd |url=https://books.google.com/books?id=NW3SAAAAMAAJ&pg=PA140}}</ref> until ] synthesis of 1910.<ref>{{cite journal | vauthors = Sölrensen SP |title=Über die Synthese des ''dl''-Arginins (α-Amino-δ-guanido-''n''-valeriansäure) und der isomeren α-Guanido-δ-amino-''n''-valeriansäure |trans-title=On the synthesis of racemic arginine (α-amino-δ-guanido-''n''-valeric acid) and of the isomeric α-guanido-δ-amino-''n''-valeric acid |language=de |journal=Berichte der Deutschen Chemischen Gesellschaft |date=January 1910 |volume=43 |issue=1 |pages=643–651 |doi=10.1002/cber.191004301109 |url=https://zenodo.org/record/2450981 }}</ref>
	The ] ] of arginine consists of a 3-carbon ] straight chain, the distal end of which is capped by a complex ] group.
			==Sources==
	]
			===Production===
			It is traditionally obtained by ] of various cheap sources of protein, such as ].<ref>{{cite journal|title=d-Arginine Hydrochloride| vauthors = Brand E, Sandberg M |journal=Org. Synth.|year=1932|volume=12|page=4|doi=10.15227/orgsyn.012.0004}}</ref> It is obtained commercially by fermentation. In this way, 25-35 g/liter can be produced, using glucose as a carbon source.<ref name=Ullmann>{{Ullmann|first1=Karlheinz|last1=Drauz|first2=Ian|last2=Grayson|first3=Axel|last3=Kleemann|first4=Hans-Peter|last4=Krimmer|first5=Wolfgang|last5=Leuchtenberger|first6=Christoph|last6=Weckbecker |display-authors=3| name-list-style = vanc |year=2006|doi=10.1002/14356007.a02_057.pub2|title=Amino Acids}}</ref>
	With a ] of 12.48, the guanidinium group is positively charged in neutral, acidic and even most basic environments, and thus imparts ] chemical properties to arginine.
	Because of the ] between the double bond and the nitrogen lone pairs, the positive charge is delocalized, enabling the formation of multiple ].
	==Sources==
	===Dietary sources===		===Dietary sources===
			Arginine is classified as a semiessential or conditionally ], depending on the developmental stage and health status of the individual.<ref name="tapiero">{{cite journal |vauthors=Tapiero H, Mathé G, Couvreur P, Tew KD | title = L-Arginine | journal = Biomedicine & Pharmacotherapy | date = November 2002 | volume = 56 | issue = 9 | pages = 439–445 | doi = 10.1016/s0753-3322(02)00284-6 | pmid = 12481980 | department = (review) }}</ref> Preterm infants are unable to synthesize arginine internally, making the amino acid nutritionally essential for them.<ref>{{cite journal | vauthors = Wu G, Jaeger LA, Bazer FW, Rhoads JM | title = Arginine deficiency in preterm infants: biochemical mechanisms and nutritional implications | journal = The Journal of Nutritional Biochemistry | volume = 15 | issue = 8 | pages = 442–51 | date = August 2004 | pmid = 15302078 | doi = 10.1016/j.jnutbio.2003.11.010 | department = (review) | doi-access = free }}</ref> Most healthy people do not need to supplement with arginine because it is a component of all protein-containing foods<ref name=mayo>{{cite web|title=Drugs and Supplements Arginine|website=]|url=http://www.mayoclinic.org/drugs-supplements/arginine/background/hrb-20058733|access-date=15 January 2015}}</ref> and can be synthesized in the body from ] via ].<ref>{{Cite book|url=https://books.google.com/books?id=3qexy5Se3SoC&pg=PA76|title=Dietitian's Handbook of Enteral and Parenteral Nutrition| vauthors = Skipper A |date=1998|publisher=Jones & Bartlett Learning|isbn=978-0-8342-0920-6|pages=76|language=en}}</ref><ref name=":1">{{Cite book|url=https://books.google.com/books?id=1nRbFrSil40C&pg=PA48|title=Enteral Nutrition| vauthors = Borlase BC |date=1994|publisher=Jones & Bartlett Learning|isbn=978-0-412-98471-6|pages=48|language=en}}</ref> Additional, dietary arginine is necessary for otherwise healthy individuals temporarily under physiological stress, for example during recovery from burns, injury or sepsis,<ref name=":1" /> or if either of the major sites of arginine biosynthesis, the ] and ]s, have reduced function, because the small bowel does the first step of the synthesizing process and the kidneys do the second.<ref name=":0" />
	'''Arginine''' is a conditionally nonessential amino acid, meaning most of the time it can be manufactured by the human body, and does not need to be obtained directly through the diet. The biosynthetic pathway however does not produce sufficient arginine, and some must still be consumed through diet. Individuals who have poor nutrition or certain physical conditions may be advised to increase their intake of foods containing arginine. Arginine is found in a wide variety of foods, including<ref>{{cite web|url=http://www.keysupplements.com/articles/L-Arginine-Supplements-Nitric-Oxide-Scientific-Studies.htm |title=L-Arginine Supplements Nitric Oxide Scientific Studies Food Sources |accessdate=2007-02-20}}</ref>:
	* Animal sources
	: dairy products (e.g., ], ], ], ], ] drinks), ], ] (e.g., bacon, ham), ] , ] (e.g. chicken and turkey light meat), ] (e.g. pheasant, quail), ] (e.g., halibut, lobster, salmon, shrimp, snails, tuna)
	* Plant sources
	: ] and flour, buckwheat, ], ], ]s, ] (coconut, pecans, cashews, walnuts, almonds, Brazil nuts, hazelnuts, pinenuts), ] (pumpkin, sesame, sunflower), ], cooked ], '']'' (canaryseed or ALPISTE)
			Arginine is an essential amino acid for birds, as they do not have a ].<ref>{{Cite book|url=https://books.google.com/books?id=dFb7AwAAQBAJ&pg=PA45|title=A Biochemical Approach to Nutrition| vauthors = Freedland RA, Briggs S |date=2012-12-06|publisher=Springer Science & Business Media|isbn=9789400957329|pages=45|language=en}}</ref> For some carnivores, for example cats, dogs<ref>{{Cite book|url=https://books.google.com/books?id=LWC6PChg9ZEC&pg=PA65|title=Nutrient Requirements of Dogs |date=1985|publisher=National Academies Press|isbn=978-0-309-03496-8|pages=65|language=en}}</ref> and ferrets, arginine is essential,<ref name=":0" /> because after a meal, their highly efficient ] produces large quantities of ] which need <!-- quantities is plural -->to be processed through the urea cycle, and if not enough arginine is present, the resulting ammonia toxicity can be lethal.<ref name=":2">{{Cite book|url=https://books.google.com/books?id=mh7yCQAAQBAJ&pg=PA232|title=Nutrition and Disease Management for Veterinary Technicians and Nurses| vauthors = Wortinger A, Burns K |date=2015-06-11|publisher=John Wiley & Sons|isbn=978-1-118-81108-5|pages=232|language=en}}</ref> This is not a problem in practice, because meat contains sufficient arginine to avoid this situation.<ref name=":2" />
	===Biosynthesis===
	Arginine is synthesized from ] by the sequential action of the cytosolic enzymes ] (ASS) and ] (ASL). In terms of energy, this is costly, as the synthesis of each molecule of argininosuccinate requires hydrolysis of ] (ATP) to ] (AMP), i.e., two ATP equivalents.
			Animal sources of arginine include meat, dairy products, and eggs,<ref>{{Cite book|url=https://books.google.com/books?id=p_YtDwAAQBAJ&pg=PA240|title=Nutrition for Sport, Exercise, and Health| vauthors = Spano MA, Kruskall LJ, Thomas DT | name-list-style = vanc |date=2017-08-30|publisher=Human Kinetics|isbn=978-1-4504-1487-6|pages=240|language=en}}</ref><ref name=":3">{{Cite book|url=https://books.google.com/books?id=kzKqMAkJw3UC&pg=PA75|title=Bioactive Dietary Factors and Plant Extracts in Dermatology| vauthors = Watson RR, Zibadi S |date=2012-11-28|publisher=Springer Science & Business Media|isbn=978-1-62703-167-7|pages=75|language=en}}</ref> and plant sources include seeds of all types, for example grains, beans, and nuts.<ref name=":3" />
	Citrulline can be derived from multiple sources:
	* from arginine via ] (NOS)
	* from ] via catabolism of ] or ]/]
	* from ] (ADMA) via DDAH
			===Biosynthesis===
	The pathways linking arginine, ], and ] are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage.
			Arginine is synthesized from ] in the urea cycle by the sequential action of the cytosolic enzymes ] and ]. This is an energetically costly process, because for each molecule of ] that is synthesized, one molecule of ] (ATP) is hydrolyzed to ] (AMP), consuming two ATP equivalents.{{cn|date=July 2024}}
			The pathways linking arginine, ], and ] are bidirectional. Thus, the net use or production of these amino acids is highly dependent on cell type and developmental stage.{{cn|date=July 2024}}
	On a whole-body basis, synthesis of arginine occurs principally via the intestinal–renal axis, wherein ]s of the ], which produce ] primarily from ] and ], collaborate with the ]s of the ], which extract citrulline from the circulation and convert it to arginine, which is returned to the circulation. As a consequence, impairment of small bowel or renal function can reduce endogenous arginine synthesis, thereby increasing the dietary requirement.
			]
	Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that also induce ]. Thus, citrulline, a coproduct of the NOS-catalyzed reaction, can be recycled to arginine in a pathway known as the citrulline-NO or arginine-citrulline pathway. This is demonstrated by the fact that in many cell types, citrulline can substitute for arginine to some degree in supporting NO synthesis. However, recycling is not quantitative because citrulline accumulates along with nitrate and nitrite, the stable end-products of NO, in NO-producing cells.<ref>{{cite journal | last1 = Morris Jr | first1 = SM | title = Enzymes of arginine metabolism. | url = http://www.nutrition.org/cgi/content/full/134/10/2743S | pmid = 15465778 | author-separator =, | journal = The Journal of nutrition | author-name-separator= | volume=134 | issue=10 Suppl | year=2004 | month=October | pages=2743S–2747S }}</ref>
			Arginine is made by the body as follows. The ]s of the ] produce citrulline, primarily from ] and ], which is secreted into the bloodstream which carries it to the ]s of the ], which extract the citrulline and convert it to arginine, which is returned to the blood. This means that impaired small bowel or renal function can reduce arginine synthesis and thus create a dietary requirement for arginine. For such a person, arginine would become "essential".
	==Function==
	Arginine plays an important role in cell division, the healing of wounds, removing ammonia from the body, immune function, and the release of hormones.<ref name="tapiero"/><ref name="stechmiller">{{cite journal | last = Stechmiller | first = J.K. | coauthors = ''et al.'' | title = Arginine supplementation and wound healing | journal = Nutrition in Clinical Practice | volume = 20 | issue = 13 | year = 2005| month = February | pages = 52–61 REVIEW | pmid = 16207646 | accessdate = 2009-11-29 | doi = 10.1177/011542650502000152 }}</ref><ref name="witte">{{cite journal | last = Witte | first = M.B. | coauthors = Barbul, A | title = Arginine physiology and its implication for wound healing | journal = Wound Repair and Regeneration | volume = 11 | issue = 6 | year = 2003| month = Nov-Dec | pages = 419–423 REVIEW | pmid = 14617280 | accessdate = 2009-11-29 | doi = 10.1046/j.1524-475X.2003.11605.x }}</ref> Arginine taken in combination with ]s<ref>{{cite journal | doi = 10.1080/00926230390155104 | last1 = Stanislavov | first1 = R. | last2 = Nikolova | first2 = V| author-separator =, | author-name-separator= | year = 2003 | title = Treatment of Erectile Dysfunction with Pycnogenol and L-arginine | url = | journal = Journal of Sex and Marital Therapy | volume = 29 | issue = 3| pages = 207–213 | pmid = 12851125 }}</ref> or ],<ref>{{cite journal | doi = 10.1016/S0302-2838(02)00175-6 | last1 = Lebret | first1 = T. | last2 = Hervéa | first2 = J. M. | last3 = Gornyb | first3 = P. | last4 = Worcelc | first4 = M. | last5 = Botto | first5 = H. | year = 2002 | title = Efficacy and Safety of a Novel Combination of L-Arginine Glutamate and Yohimbine Hydrochloride: A New Oral Therapy for Erectile Dysfunction | url = | journal = European Urology | volume = 41 | issue = 6| pages = 608–613 | pmid = 12074777 }}</ref> has also been used as a treatment for ].
			Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that increase the production of ]. This allows citrulline, a byproduct of the NOS-catalyzed production of nitric oxide, to be recycled to arginine in a pathway known as the citrulline to nitric oxide (citrulline-NO) or arginine-citrulline pathway. This is demonstrated by the fact that, in many cell types, nitric oxide synthesis can be supported to some extent by citrulline, and not just by arginine. This recycling is not quantitative, however, because citrulline accumulates in nitric oxide producing cells along with ] and ], the stable end-products of nitric oxide breakdown.<ref>{{cite journal | vauthors = Morris SM | title = Enzymes of arginine metabolism | journal = The Journal of Nutrition | volume = 134 | issue = 10 Suppl | pages = 2743S–2747S; discussion 2765S–2767S | date = October 2004 | pmid = 15465778 | doi = 10.1093/jn/134.10.2743S | department = (review) | doi-access = free }}</ref>
	The benefits and functions attributed to oral supplementation of L-arginine include:
	* Precursor for the synthesis of ] (NO)<ref>{{cite journal | last = Andrew | first = P.J. | coauthors = Myer, B. | title = Enzymatic function of nitric oxide synthases | journal = Cardiovascular Research | volume = 43 | issue = 3 | year = 1999 | month = August 15 | pages = 521–531 REVIEW | pmid = 10690324 | doi = 10.1016/S0008-6363(99)00115-7 | accessdate = 2009-11-29 }} </ref>
			== Function ==
	* Reduces healing time of injuries (particularly bone)<ref name="stechmiller"/><ref name="witte"/>
			Arginine plays an important role in ], ], removing ammonia from the body, ],<ref>{{Cite book|url=https://books.google.com/books?id=Hc3rCgAAQBAJ&pg=PA17|title=The Metabolic Challenges of Immune Cells in Health and Disease| vauthors = Mauro C, Frezza C |date=2015-07-13|publisher=Frontiers Media SA|isbn=9782889196227|pages=17|language=en}}</ref> and the release of hormones.<ref name="tapiero"/><ref>{{cite journal | vauthors = Stechmiller JK, Childress B, Cowan L | title = Arginine supplementation and wound healing | journal = Nutrition in Clinical Practice | volume = 20 | issue = 1 | pages = 52–61 | date = February 2005 | pmid = 16207646 | doi = 10.1177/011542650502000152 | department = (review) }}</ref><ref>{{cite journal | vauthors = Witte MB, Barbul A | title = Arginine physiology and its implication for wound healing | journal = Wound Repair and Regeneration | volume = 11 | issue = 6 | pages = 419–23 | year = 2003 | pmid = 14617280 | doi = 10.1046/j.1524-475X.2003.11605.x | s2cid = 21239136 | department = (review) }}</ref> It is a precursor for the synthesis of ] (NO),<ref>{{cite journal | vauthors = Andrew PJ, Mayer B | title = Enzymatic function of nitric oxide synthases | journal = Cardiovascular Research | volume = 43 | issue = 3 | pages = 521–31 | date = August 1999 | pmid = 10690324 | doi = 10.1016/S0008-6363(99)00115-7 | department = (review) | doi-access = free}}</ref> making it important in the regulation of ].<ref>{{cite journal | vauthors = Gokce N | title = L-arginine and hypertension | journal = The Journal of Nutrition | volume = 134 | issue = 10 Suppl | pages = 2807S–2811S; discussion 2818S–2819S | date = October 2004 | pmid = 15465790 | doi = 10.1093/jn/134.10.2807S | doi-access = free }}</ref><ref>{{cite journal | vauthors = Kibe R, Kurihara S, Sakai Y et al | title = Upregulation of colonic luminal polyamines produced by intestinal microbiota delays senescence in mice | journal = Scientific Reports | volume = 4 | issue = 4548 | date = 2014 | page = 4548 | pmid = 24686447| doi = 10.1038/srep04548 | pmc = 4070089 | bibcode = 2014NatSR...4E4548K | doi-access = free }}</ref> Arginine is necessary for T-cells to function in the body, and can lead to their deregulation if depleted.<ref>{{Cite journal |last1=Banerjee |first1=Kasturi |last2=Chattopadhyay |first2=Agnibha |last3=Banerjee |first3=Satarupa |date=2022-07-01 |title=Understanding the association of stem cells in fetal development and carcinogenesis during pregnancy |journal=Advances in Cancer Biology - Metastasis |language=en |volume=4 |pages=100042 |doi=10.1016/j.adcanc.2022.100042 |s2cid=248485831 |issn=2667-3940|doi-access=free}}</ref><ref>{{Cite journal |last1=Rodriguez |first1=Paulo C. |last2=Quiceno |first2=David G. |last3=Ochoa |first3=Augusto C. |date=2006-10-05 |title=l-arginine availability regulates T-lymphocyte cell-cycle progression |url=https://doi.org/10.1182/blood-2006-06-031856 |journal=Blood |volume=109 |issue=4 |pages=1568–1573 |doi=10.1182/blood-2006-06-031856 |issn=0006-4971 |pmc=1794048 |pmid=17023580}}</ref>
	* Quickens repair time of damaged tissue<ref name="stechmiller"/><ref name="witte"/>
	* Helps decrease ]<ref>{{cite journal | last = Gokce | first = N.. | title = L-Arginine and hypertension | journal = Journal of Nutrition | volume = 134 | issue = 10 Suppl | year = 2004| month = October | pages = 2807S–2811S REVIEW | pmid = 15465790 | accessdate = 2009-11-29 }}</ref><ref>{{cite journal | last = Rajapakse | first = N.W. | coauthors = ''et al.'' | title = Exogenous L-arginine ameliorates angiotensin II-induced hypertension and renal damage in rats | journal = Hypertension | volume = 52 | issue = 6 | year = 2008 | month = December | pages = 1084–1090 | pmid = 18981330 | doi = 10.1161/HYPERTENSIONAHA.108.114298 | accessdate = 2009-11-29 | pmc = 2680209 }} </ref>
	===Proteins===		===Proteins===
			Arginine's side chain is ], because at physiological pH it contains a positively charged guanidinium group, which is highly polar, at the end of a hydrophobic ] hydrocarbon chain. Because globular proteins have hydrophobic interiors and hydrophilic surfaces,<ref>{{Cite book |title=Biochemistry|url=https://archive.org/details/biochemistry0003math|url-access=registration| vauthors = Mathews CK, Van Holde KE, Ahern KG |date=2000|publisher=Benjamin Cummings|isbn=978-0805330663|edition=3rd|location=San Francisco, Calif.|pages=|oclc=42290721}}</ref> arginine is typically found on the outside of the protein, where the hydrophilic head group can interact with the polar environment, for example taking part in ]ing and ]<ref name=":4">{{Cite book|url=https://books.google.com/books?id=CN9sYPJdXs4C&pg=PA326|title=Bioinformatics for Geneticists: A Bioinformatics Primer for the Analysis of Genetic Data| vauthors = Barnes MR |date=2007-04-16|publisher=John Wiley & Sons|isbn=9780470026199 |pages=326 }}</ref> For this reason, it is frequently found at the interface between two proteins.<ref>{{Cite book|url=https://books.google.com/books?id=hbd8dlG7zkIC&pg=PA13|title=Protein-protein Recognition| vauthors = Kleanthous C |date=2000|publisher=Oxford University Press|isbn=9780199637607|pages=13|language=en}}</ref> The aliphatic part of the side chain sometimes remains below the surface of the protein.<ref name=":4" />
	The distributing basics of the moderate structure found in geometry, charge distribution and ability to form multiple H-bonds make arginine ideal for binding negatively charged groups. For this reason, arginine prefers to be on the outside of the proteins where it can interact with the polar environment.
			Arginine residues in proteins can be deiminated by PAD enzymes to form citrulline, in a ] process called ].This is important in fetal development, is part of the normal immune process, as well as the control of gene expression, but is also significant in ]s.{{sfn|Griffiths|Unwin|2016|p=275}} Another post-translational modification of arginine involves ] by protein ]s.{{sfn|Griffiths|Unwin|2016|p=176}}
	Incorporated in proteins, arginine can also be converted to citrulline by PAD enzymes. In addition, arginine can be ] by protein methyltransferases.
	===Precursor===		===Precursor===
			Arginine is the immediate precursor of nitric oxide, an important signaling molecule which can act as a ], as well as an intercellular messenger which regulates vasodilation, and also has functions in the immune system's reaction to infection.{{cn|date=July 2024}}
	Arginine is the immediate precursor of ], ], ], and ]; is necessary for the synthesis of ]; and can also be used for the synthesis of ]s (mainly through ornithine and to a lesser degree through agmatine), ], and ]. As a precursor of nitric oxide, arginine may have a role in the treatment of some conditions where ] is required.<ref name="tapiero"/> The presence of ] (ADMA), a close relative, inhibits the nitric oxide reaction; therefore, ADMA is considered a marker for ], just as L-arginine is considered a sign of a healthy ].
			Arginine is also a precursor for ], ], and ]; is necessary for the synthesis of ]; and can also be used for the synthesis of ]s (mainly through ornithine and to a lesser degree through agmatine, citrulline, and glutamate). The presence of ] (ADMA), a close relative, inhibits the nitric oxide reaction; therefore, ADMA is considered a marker for ], just as <small>L</small>-arginine is considered a sign of a healthy ].<ref name="pmid32781796">{{cite journal |vauthors=Gambardella J, Khondkar W, Morelli MB, Wang X, Santulli G, Trimarco V |title=Arginine and Endothelial Function |journal=Biomedicines |volume=8 |issue=8 |date=August 2020 |page=277 |pmid=32781796 |pmc=7460461 |doi=10.3390/biomedicines8080277 |url= |doi-access=free }}</ref>
	===Treatment of dentin hypersensitivity===
	Arginine (8%) in dental products (e.g., ]) provides effective relief from sensitive teeth by depositing a ]-like ], containing ] and ], within the dentin tubules and in a protective layer on the dentin surface.<ref name="petrou">{{cite journal | last = Petrou | first = I. | coauthors = ''et al.'' | title = A breakthrough therapy for dentin hypersensitivity: how dental products containing 8% arginine and calcium carbonate work to deliver effective relief of sensitive teeth. | journal = The Journal of Clinical Dentisry | volume = 20 | issue = 1 | year = 2009 | month = | pages = 23–31 | pmid = 19489189 | accessdate = 2011-5-2 | doi=}}</ref>
			== Structure ==
	===Treatment of herpes simplex virus===
			]
	An unproven claim is that a low ratio of arginine to ] may be of benefit in the treatment of herpes simplex virus.
			The ] ] of arginine consists of a 3-carbon ] straight chain, the distal end of which is capped by a ] group, which has a ] of 13.8,<ref>{{cite journal | vauthors = Fitch CA, Platzer G, Okon M, Garcia-Moreno BE, McIntosh LP |display-authors=3| title = Arginine: Its pKa value revisited | journal = Protein Science | volume = 24 | issue = 5 | pages = 752–61 | date = May 2015 | pmid = 25808204 | pmc = 4420524 | doi = 10.1002/pro.2647 }}</ref> and is therefore always protonated and positively charged at physiological pH. Because of the ] between the double bond and the nitrogen ]s, the positive charge is delocalized, enabling the formation of multiple ]s.
	For more information, refer to ] also see journal article.<ref>{{cite journal |year=2009 |month=April |title= Antiviral effect of arginine against herpes simplex virus type 1 |source=International Journal of Molecular Medicine |volume= 23 |issue= 4 |pages= 495–499 |journal=International Journal of Molecular Medicine |pmid= 19288025|doi= 10.3892/ijmm_00000156 |url= http://www.spandidos-publications.com/ijmm/article.jsp?article_id=ijmm_23_4_495 |accessdate=2010-10-18 |quote= |author=Takeshi Naito, Hiroshi Irie, Kazuko Tsujimoto, Keiko Ikeda, Tsutomu Arakawa, A. Hajime Koyama }}</ref>
			==Research==
	===Possible increased risk of death after supplementation following heart attack===
			===Growth hormone===
	A clinical trial found that patients taking an L-arginine supplement following a heart attack found no change in the heart's vascular tone or decrease in the symptoms of ] (the hearts' ability to pump). In fact, six more patients who were taking L-arginine died than those taking a placebo resulting in early termination of the study with the recommendation that the supplement not be used by heart attack patients.<ref></ref><ref>{{cite journal | last1 = Schulman | first1 = SP | last2 = Becker | first2 = LC | last3 = Kass | first3 = DA | last4 = Champion | first4 = HC | last5 = Terrin | first5 = ML | last6 = Forman | first6 = S | last7 = Ernst | first7 = KV | last8 = Kelemen | first8 = MD | last9 = Townsend | first9 = SN | title = L-arginine therapy in acute myocardial infarction: the Vascular Interaction With Age in Myocardial Infarction (VINTAGE MI) randomized clinical trial. | url = http://jama.ama-assn.org/cgi/content/short/295/1/58 | pmid = 16391217 | author-separator =, | journal = JAMA : the journal of the American Medical Association | author-name-separator= | doi=10.1001/jama.295.1.58 | volume=295 | issue=1 | year=2006 | month=January | pages=58–64}}</ref><ref>This study has been discussed in some detail in : "Reverse Heart Disease Now" by Stephen T Sinatra MD and James C Roberts MD, publ. Wiley 2006 ISBN 0-471-74704-1 at pp 111-113.</ref> Despite these findings, the supplement is still widely marketed as "beneficial" for the heart.
			Intravenously administered arginine is used in growth hormone stimulation tests<ref>{{MedlinePlusEncyclopedia|003377|Growth hormone stimulation test}}</ref> because it stimulates the secretion of ].<ref>{{cite journal | vauthors = Alba-Roth J, Müller OA, Schopohl J, von Werder K | s2cid = 7488757 | title = Arginine stimulates growth hormone secretion by suppressing endogenous somatostatin secretion | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 67 | issue = 6 | pages = 1186–9 | date = December 1988 | pmid = 2903866 | doi = 10.1210/jcem-67-6-1186 }}</ref> A review of clinical trials concluded that oral arginine increases growth hormone, but decreases growth hormone secretion, which is normally associated with exercising.<ref>{{cite journal | vauthors = Kanaley JA | title = Growth hormone, arginine and exercise | journal = Current Opinion in Clinical Nutrition and Metabolic Care | volume = 11 | issue = 1 | pages = 50–4 | date = January 2008 | pmid = 18090659 | doi = 10.1097/MCO.0b013e3282f2b0ad | s2cid = 22842434 }}</ref> However, a more recent trial reported that although oral arginine increased plasma levels of <small>L</small>-arginine it did not cause an increase in growth hormone.<ref>{{cite journal | vauthors = Forbes SC, Bell GJ | title = The acute effects of a low and high dose of oral L-arginine supplementation in young active males at rest | journal = Applied Physiology, Nutrition, and Metabolism| volume = 36 | issue = 3 | pages = 405–11 | date = June 2011 | pmid = 21574873 | doi = 10.1139/h11-035 }}</ref>
			===Herpes-Simplex Virus (Cold sores)===
	==Potential medical uses==
			Research from 1964 into amino acid requirements of ] in human cells indicated that "...the lack of arginine or ], and possibly the presence of ], would interfere markedly with virus synthesis", but concludes that "no ready explanation is available for any of these observations".<ref>{{cite journal | vauthors = Tankersley RW |title=Amino Acid Requirements of Herpes Simplex Virus in Human Cells |journal=Journal of Bacteriology |date=March 1964 |volume=87 |issue=3 |pages=609–613 |doi=10.1128/jb.87.3.609-613.1964 |pmid=14127578 |pmc=277062 |doi-access=free }}</ref>
	===Lung inflammation and asthma===
	The Mayo Clinic web page on L-arginine reports that inhalation of L-arginine can increase lung inflammation and worsen asthma.<ref>Sapienza MA, Kharitonov SA, Horvath I, Chung KF, Barnes PJ. "Effect of inhaled L-arginine on exhaled nitric oxide in normal and asthmatic subjects." Thorax. 1998 Mar;53(3):172-5.</ref>
			Further reviews conclude that "lysine's efficacy for ] may lie more in prevention than treatment." and that "the use of lysine for decreasing the severity or duration of outbreaks" is not supported, while further research is needed.<ref>{{cite journal | vauthors = Tomblin FA, Lucas KH | title = Lysine for management of herpes labialis | journal = American Journal of Health-System Pharmacy | volume = 58 | issue = 4 | pages = 298–300, 304 | date = February 2001 | pmid = 11225166 | doi = 10.1093/ajhp/58.4.298 | doi-access = free }}</ref> A 2017 study concludes that "clinicians could consider advising patients that there is a theoretical role of lysine supplementation in the prevention of herpes simplex sores but the research evidence is insufficient to back this. Patients with cardiovascular or gallbladder disease should be cautioned and warned of the theoretical risks."<ref>{{cite journal | vauthors = Mailoo VJ, Rampes S | title = Lysine for Herpes Simplex Prophylaxis: A Review of the Evidence | journal = Integrative Medicine | volume = 16 | issue = 3 | pages = 42–46 | date = June 2017 | pmid = 30881246 | pmc = 6419779 }}</ref>
	===Growth hormone===
	Arginine may stimulate the secretion of ],<ref name="alba-roth">{{cite journal |author=Alba-Roth J, Müller O, Schopohl J, von Werder K |title=Arginine stimulates growth hormone secretion by suppressing endogenous somatostatin secretion |journal=J Clin Endocrinol Metab |volume=67 |issue=6 |pages=1186–9 |year=1988 |pmid=2903866 |doi=10.1210/jcem-67-6-1186}}</ref> and is used in growth hormone stimulation tests.<ref>U.S. National Library of Medicine (September 2009). </ref>. However, more recent research suggests that are ineffective at increasing growth hormone levels despite being effective at increasing plasma levels of l-arginine.
	===MELAS syndrome===		===High blood pressure===
			A meta-analysis showed that <small>L</small>-arginine reduces blood pressure with pooled estimates of 5.4 mmHg for systolic blood pressure and 2.7 mmHg for diastolic blood pressure.<ref>{{cite journal | vauthors = Dong JY, Qin LQ, Zhang Z, Zhao Y, Wang J, Arigoni F, Zhang W |display-authors=3| title = Effect of oral L-arginine supplementation on blood pressure: a meta-analysis of randomized, double-blind, placebo-controlled trials | journal = American Heart Journal | volume = 162 | issue = 6 | pages = 959–65 | date = December 2011 | pmid = 22137067 | doi = 10.1016/j.ahj.2011.09.012 | department = review }}</ref>
	Several trials delved into effects of L-arginine in ], a ].<ref name="pmid16769961">{{cite journal |author=Koga Y, Akita Y, Junko N, Yatsuga S, Povalko N, Fukiyama R, Ishii M, Matsuishi T |title=Endothelial dysfunction in MELAS improved by l-arginine supplementation |journal=] |volume=66 |issue=11 |pages=1766–9 |year=2006 |month=June |pmid=16769961 |doi=10.1212/01.wnl.0000220197.36849.1e |url=http://www.neurology.org/cgi/pmidlookup?view=long&pmid=16769961}}</ref><ref name="pmid19198147">{{cite journal |author=Koga Y |title= |language=Japanese |journal=] |volume=48 |issue=11 |pages=1010–2 |year=2008 |month=November |pmid=19198147 |doi= |url=}}</ref><ref name="pmid17276739">{{cite journal |author=Koga Y, Akita Y, Nishioka J, Yatsuga S, Povalko N, Katayama K, Matsuishi T |title=MELAS and L-arginine therapy |journal=] |volume=7 |issue=1–2 |pages=133–9 |year=2007 |pmid=17276739 |doi=10.1016/j.mito.2006.11.006 |url=http://linkinghub.elsevier.com/retrieve/pii/S1567-7249(06)00227-3}}</ref><ref name="pmid19780807">{{cite journal |author=Finsterer J |title=Management of mitochondrial stroke-like-episodes |journal=] |volume=16 |issue=11 |pages=1178–84 |year=2009 |month=November |pmid=19780807 |doi=10.1111/j.1468-1331.2009.02789.x |url=http://www3.interscience.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=1351-5101&date=2009&volume=16&issue=11&spage=1178}}</ref>
			Supplementation with {{sm|l}}-arginine reduces ] and lengthens pregnancy for women with ], including women with high blood pressure as part of ]. It did not lower systolic blood pressure or improve ].<ref>{{cite journal | vauthors = Gui S, Jia J, Niu X, Bai Y, Zou H, Deng J, Zhou R |display-authors=3| title = Arginine supplementation for improving maternal and neonatal outcomes in hypertensive disorder of pregnancy: a systematic review | journal = Journal of the Renin-Angiotensin-Aldosterone System | volume = 15 | issue = 1 | pages = 88–96 | date = March 2014 | pmid = 23435582 | doi = 10.1177/1470320313475910 | department = (review) | doi-access = free }}</ref>
	===Sepsis===
	Cellular arginine biosynthetic capacity determined by activity of ] (AS) is induced by the same mediators of ] response — ] and ]s — that induce ] (NOS), the ] responsible for ] synthesis.<ref>{{cite journal |year=1995 |month= |title= ROLE OF ARGININE SYNTHESIS IN SURGICAL SEPSIS |source=Crisp Data Base National Institutes Of Health |volume= |issue= |pages= |pmid= |doi= |url= http://toxnet.nlm.nih.gov/ |accessdate=2010-02-22 |quote= |author=MORRIS SM }}</ref>
	===Malate salt===		===Schizophrenia===
			Both liquid chromatography and liquid chromatography/mass spectrometric assays have found that brain tissue of deceased people with ] shows altered arginine metabolism. Assays also confirmed significantly reduced levels of γ-aminobutyric acid (GABA), but increased ] concentration and glutamate/GABA ratio in the schizophrenia cases. Regression analysis indicated positive correlations between arginase activity and the age of disease onset and between L-ornithine level and the duration of illness. Moreover, cluster analyses revealed that L-arginine and its main metabolites L-citrulline, L-ornithine and agmatine formed distinct groups, which were altered in the schizophrenia group. Despite this, the biological basis of schizophrenia is still poorly understood, a number of factors, such as dopamine hyperfunction, glutamatergic hypofunction, GABAergic deficits, cholinergic system dysfunction, stress vulnerability and neurodevelopmental disruption, have been linked to the aetiology and/or pathophysiology of the disease.<ref>{{cite journal | vauthors = Liu P, Jing Y, Collie ND, Dean B, Bilkey DK, Zhang H |display-authors=3| title = Altered brain arginine metabolism in schizophrenia | journal = Translational Psychiatry | volume = 6 | issue = 8 | pages = e871 | date = August 2016 | pmid = 27529679 | pmc = 5022089 | doi = 10.1038/tp.2016.144 | doi-access = free }}</ref>
	The ] ] of arginine can also be used during the treatment of alcoholic hepatitis and advanced cirrhosis.<ref>{{cite journal |year=1970 |month= May–June|title= Therapeutic effects of arginine malate in alcoholic cirrhosis |journal= Therapie |volume=25 |issue= 3 |pages=629–33 |pmid= 5431854|doi= |url= |accessdate=2010-02-22 |quote= |author= Tissot-Favre A, Brette R }}</ref>
	===Pre-eclampsia ===		===Raynaud's phenomenon===
			Oral L-arginine has been shown to reverse digital necrosis in ]<ref>{{Cite journal |last1=Rembold |first1=Christopher M. |last2=Ayers |first2=Carlos R. |date=February 2003 |title=Oral L-arginine can reverse digital necrosis in Raynaud's phenomenon |url=https://pubmed.ncbi.nlm.nih.gov/12701823/ |journal=Molecular and Cellular Biochemistry |volume=244 |issue=1–2 |pages=139–141 |doi=10.1023/A:1022422932108 |issn=0300-8177 |pmid=12701823|s2cid=30249281 }}</ref>
	A preliminary study of supplementation with L-arginine and antioxidant vitamins showed that this combination may help to combat abnormally high blood pressure during high risk pregnancies.<ref>{{cite journal | author = Vadillo-Ortega F ''et al.'' | year = 2011 | title = Effect of supplementation during pregnancy with L-arginine and antioxidant vitamins in medical food on pre-eclampsia in high risk population: randomised controlled trial | journal = British Medical Journal | volume = 342 | doi = 10.1136/bmj.d2901 | url = http://www.bmj.com/content/342/bmj.d2901 | pages = d2901–d2901}}</ref>
			==Safety and potential drug interactions==
			L-arginine is recognized as safe (GRAS-status) at intakes of up to 20 grams per day.<ref>{{cite journal | vauthors = Shao A, Hathcock JN | title = Risk assessment for the amino acids taurine, L-glutamine and L-arginine | journal = Regulatory Toxicology and Pharmacology | volume = 50 | issue = 3 | pages = 376–99 | date = April 2008 | pmid = 18325648 | doi = 10.1016/j.yrtph.2008.01.004 }}</ref> L-arginine is found in many foods, such as fish, poultry, and dairy products, and is used as a dietary supplement.<ref name="mlp">{{Cite web|title=L-Arginine|url=https://medlineplus.gov/druginfo/natural/875.html|access-date=2021-05-27|publisher=MedlinePlus, US National Institutes of Health|date=13 October 2021|language=en}}</ref> It may interact with various ]s and herbal supplements.<ref name=mlp/>
	==See also==		==See also==
			* ]
	* ]		* ]
	* ] and ] are toxic analogues of arginine and ornithine		* ] and ] are toxic ] of arginine and ].
	==References==		==References==
	{{Reflist|2}}		{{reflist}}
			==Sources==
			* {{cite book | vauthors = Griffiths JR, Unwin RD |title=Analysis of Protein Post-Translational Modifications by Mass Spectrometry |date=2016 |publisher=John Wiley & Sons |isbn=978-1-119-25088-3 }}
	==External links==		== External links ==
	{{Commons category|arginine}}		{{Commons category|Arginine}}
	*		*
	*		*
	*
	{{AminoAcids}}		{{Amino acids}}
	{{Amino acid metabolism intermediates}}		{{Amino acid metabolism intermediates}}
			{{Nitric oxide signaling}}
			{{Authority control}}
	]		]
	]		]
			]
	]		]
	]
	]		]
	]		]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]
	]