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Cas Database

372-75-8

372-75-8

Identification

  • Product Name:L(+)-Citrulline

  • CAS Number: 372-75-8

  • EINECS:206-759-6

  • Molecular Weight:175.188

  • Molecular Formula: C6H13N3O3

  • HS Code:29241900

  • Mol File:372-75-8.mol

Synonyms:L-Citrullin;L-Cit-OH;L-Citrulline;N5-(Aminocarbonyl)ornithine;L-Citrulline (Fermentation);H-Cit-OH;.delta.-Ureidonorvaline;2-Amino-5-uredovaleric acid;Ngamma-carbamylornithine;delta-Ureidonorvaline;N~5~-(aminocarbonyl)ornithine;2-amino-5-(carbamoylamino)pentanoic acid;L-Citrulline;(2S)-2-amino-5-(carbamoylamino)pentanoic acid;Ornithine, N5-carbamoyl-, L- (8CI);L-Ornithine, N5-(aminocarbonyl)-;Ornithine, N5-(aminocarbonyl)-;Citrulline, L-;Ornithine, N5-carbamoyl-, L-;Citrulline;L-Ornithine,N5-(aminocarbonyl)-;.alpha.-Amino-.delta.-ureidovaleric acid;N5-(Aminocarbonyl)-L-ornithine;alpha-Amino-delta-ureidovaleric acid;N(.delta.)-Carbamylornithine;

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Safety information and MSDS view more

  • Pictogram(s):IrritantXi

  • Hazard Codes:Xi

  • Signal Word:Warning

  • Hazard Statement:H315 Causes skin irritationH319 Causes serious eye irritation

  • First-aid measures: General adviceConsult a physician. Show this safety data sheet to the doctor in attendance.If inhaled If breathed in, move person into fresh air. If not breathing, give artificial respiration. Consult a physician. In case of skin contact Wash off with soap and plenty of water. Consult a physician. In case of eye contact Rinse thoroughly with plenty of water for at least 15 minutes and consult a physician. If swallowed Never give anything by mouth to an unconscious person. Rinse mouth with water. Consult a physician.

  • Fire-fighting measures: Suitable extinguishing media Use water spray, alcohol-resistant foam, dry chemical or carbon dioxide. Wear self-contained breathing apparatus for firefighting if necessary.

  • Accidental release measures: Use personal protective equipment. Avoid dust formation. Avoid breathing vapours, mist or gas. Ensure adequate ventilation. Evacuate personnel to safe areas. Avoid breathing dust. For personal protection see section 8. Prevent further leakage or spillage if safe to do so. Do not let product enter drains. Discharge into the environment must be avoided. Pick up and arrange disposal. Sweep up and shovel. Keep in suitable, closed containers for disposal.

  • Handling and storage: Avoid contact with skin and eyes. Avoid formation of dust and aerosols. Avoid exposure - obtain special instructions before use.Provide appropriate exhaust ventilation at places where dust is formed. For precautions see section 2.2. Store in cool place. Keep container tightly closed in a dry and well-ventilated place.

  • Exposure controls/personal protection:Occupational Exposure limit valuesBiological limit values Handle in accordance with good industrial hygiene and safety practice. Wash hands before breaks and at the end of workday. Eye/face protection Safety glasses with side-shields conforming to EN166. Use equipment for eye protection tested and approved under appropriate government standards such as NIOSH (US) or EN 166(EU). Skin protection Wear impervious clothing. The type of protective equipment must be selected according to the concentration and amount of the dangerous substance at the specific workplace. Handle with gloves. Gloves must be inspected prior to use. Use proper glove removal technique(without touching glove's outer surface) to avoid skin contact with this product. Dispose of contaminated gloves after use in accordance with applicable laws and good laboratory practices. Wash and dry hands. The selected protective gloves have to satisfy the specifications of EU Directive 89/686/EEC and the standard EN 374 derived from it. Respiratory protection Wear dust mask when handling large quantities. Thermal hazards

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  • Manufacture/Brand:Usbiological
  • Product Description:L-Citrulline-d7
  • Packaging:1mg
  • Price:$ 460
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  • Manufacture/Brand:TRC
  • Product Description:L-Citrulline
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  • Manufacture/Brand:TCI Chemical
  • Product Description:L-Citrulline >98.0%(T)
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  • Manufacture/Brand:TCI Chemical
  • Product Description:L-Citrulline >98.0%(T)
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  • Product Description:L-Citrulline United States Pharmacopeia (USP) Reference Standard
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  • Product Description:L-Citrulline ≥98% (TLC)
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Relevant articles and documentsAll total 30 Articles be found

Dissecting structural and electronic effects in inducible nitric oxide synthase

Hannibal, Luciana,Page, Richard C.,Haque, Mohammad Mahfuzul,Bolisetty, Karthik,Yu, Zhihao,Misra, Saurav,Stuehr, Dennis J.

, p. 153 - 165 (2015)

Nitric oxide synthases (NOSs) are haem-thiolate enzymes that catalyse the conversion of L-arginine (L-Arg) into NO and citrulline. Inducible NOS (iNOS) is responsible for delivery of NO in response to stressors during inflammation. The catalytic performance of iNOS is proposed to rely mainly on the haem midpoint potential and the ability of the substrate L-Arg to provide a hydrogen bond for oxygen activation (O-O scission). We present a study of native iNOS compared with iNOS-mesohaem, and investigate the formation of a low-spin ferric haem-aquo or -hydroxo species (P) in iNOS mutant W188H substituted with mesohaem. iNOS-mesohaem and W188H-mesohaem were stable and dimeric, and presented substrate-binding affinities comparable to those of their native counterparts. Single turnover reactions catalysed by iNOSoxy with L-Arg (first reaction step) or N-hydroxy-L-arginine (second reaction step) showed that mesohaem substitution triggered higher rates of FeIIO2 conversion and altered other key kinetic parameters. We elucidated the first crystal structure of a NOS substituted with mesohaem and found essentially identical features compared with the structure of iNOS carrying native haem. This facilitated the dissection of structural and electronic effects. Mesohaem substitution substantially reduced the build-up of species P in W188H iNOS during catalysis, thus increasing its proficiency towards NO synthesis. The marked structural similarities of iNOSoxy containing native haem or mesohaem indicate that the kinetic behaviour observed in mesohaem-substituted iNOS is most heavily influenced by electronic effects rather than structural alterations.

Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase

Tejero, Jesus,Biswas, Ashis,Haque, Mohammad Mahfuzul,Wang, Zhi-Qiang,Hemann, Craig,Varnado, Cornelius L.,Novince, Zachary,Hille, Russ,Goodwin, Douglas C.,Stuehr, Dennis J.

, p. 163 - 174 (2011)

NOSs (NO synthases, EC 1.14.13.39) are haem-thiolate enzymes that catalyse a two-step oxidation of L-arginine to generate NO. The structural and electronic features that regulate their NO synthesis activity are incompletely understood. To investigate how haem electronics govern the catalytic properties of NOS, we utilized a bacterial haem transporter protein to overexpress a mesohaem-containing nNOS (neuronal NOS) and characterized the enzyme using a variety of techniques. Mesohaem-nNOS catalysed NO synthesis and retained a coupled NADPH consumption much like the wild-type enzyme. However, mesohaem-nNOS had a decreased rate of Fe(III) haem reduction and had increased rates for haem-dioxy transformation, Fe(III) haem-NO dissociation and Fe(II) haem-NO reaction with O2. These changes are largely related to the 48 mV decrease in haem midpoint potential that we measured for the bound mesohaem cofactor. Mesohaem nNOS displayed a significantly lower Vmax and KmO2 value for its NO synthesis activity compared with wild-type nNOS. Computer simulation showed that these altered catalytic behaviours of mesohaem-nNOS are consistent with the changes in the kinetic parameters. Taken together, the results of the present study reveal that several key kinetic parameters are sensitive to changes in haem electronics in nNOS, and show how these changes combine to alter its catalytic behaviour. The Authors Journal compilation

Neuronal nitric oxide synthase isoforms α and μ are closely related calpain-sensitive proteins

Laine, Romuald,Ortiz De Montellano, Paul R.

, p. 305 - 312 (1998)

The neuronal nitric oxide synthase isoform nNOSμ, which is expressed in striated muscle, differs from nNOSα, the major brain isoform, by the insertion of 34 amino acid residues between the calmodulin- and flavin- binding domains [J Biol Chem 271:11204-11208 (1996)]. We show here that recombinant, purified nNOSμ, despite the peptide insertion, has the same spectroscopic properties, L-arginine k(cat) and K(m) values, optimal pH, and calmodulin binding affinity constant as nNOSα. However, nNOSμ consumes NADPH and reduces cytochrome c at approximately half the rate of nNOSα. The rates of degradation of the two proteins by rat brain and muscle homogenates show that nNOSμ is degraded more slowly than nNOSα. The in vitro half- lives of nNOSα and nNOSμ are 12 and 50 min, respectively, and calpain is important for this degradation. These short in vitro half-lives suggest that the nNOS isoforms are susceptible to rapid degradation in vivo. The elevated (20-fold) levels of calpain in diseased muscle tissue in Duchenne muscular dystrophy, and the hydrolytic sensitivity of both nNOSμ and nNOSα to this enzyme, may contribute to the deficiency of nNOS activity in the diseased tissue.

Arginine Deiminase Uses an Active-Site Cysteine in Nucleophilic Catalysis of L-Arginine Hydrolysis

Lu, Xuefeng,Galkin, Andrey,Herzberg, Osnat,Dunaway-Mariano, Debra

, p. 5374 - 5375 (2004)

Arginine deiminase (EC 3.5.3.6) catalyzes the hydrolysis of l-arginine to citrulline and ammonium ion, which is the first step of the microbial l-arginine degradation pathway. The deiminase conserves the active-site Cys-His-Asp motif found in several related enzymes that catalyze group-transfer reactions from the guanidinium center of arginine-containing substrates. For each of these enzymes, nucleophilic catalysis by the conserved Cys has been postulated but never tested. In this communication we report the results from rapid quench studies of single-turnover reactions carried out with recombinant Pseudomonas aeruginosa arginine deiminase and limiting [14C-1]l-arginine. The citrulline-formation and arginine-decay curves measured at 25 °C were fitted to yield apparent rate constants k = 3.6 ± 0.1 s-1 and k = 4.2 ± 0.1 s-1, respectively. The time course for the formation (k =13 s-1) and decay (k = 6.5 s-1) of 14C-labeled enzyme defined a kinetically competent intermediate. Under the same reaction conditions, the Cys406Ser mutant failed to form the 14C-labeled enzyme intermediate. These results, along with the recently reported enzyme X-ray structure (Galkin, A.; Kulakova, L.; Sarikaya, E.; Lim, K.; Howard, A.; Herzberg, O. J. Biol. Chem. 2004, 279, 14001-14008, evidence a reaction pathway in which l-arginine deimination proceeds via a covalent enzyme intermediate formed by ammonia displacement from the arginine guanidinum carbon by the active-site Cys406. Copyright

Directed evolution of an antitumor drug (Arginine Deiminase PpADI) for Increased Activity at Physiological pH

Zhu, Leilei,Tee, Kang Lan,Roccatano, Danilo,Sonmez, Burcu,Ni, Ye,Sun, Zhi-Hao,Schwaneberg, Ulrich

, p. 691 - 697 (2010)

Arginine deiminase (ADI; EC 3.5.3.6) has been studied as a potential antitumor drug for the treatment of arginine-auxotrophic tumors, such as hepatocellular carcinomas (HCCs) and melanomas. Studies with human lymphatic leukemia cell lines confirmed that ADI is an antiangiogenic agent for treating leukemia. The main limitation of ADI from Pseudomonas plecoglossicida (PpADI) lies in its pH-dependent activity profile, its pH optimum is at 6.5. A pH shift from 6.5 to 7.5 results in an approximately 80% drop in activity. (The pH of human plasma is 7.35 to 7.45.) In order to shift the PpADI pH optimum, a directed-evolution protocol based on an adapted citrulline-screening protocol in microtiter-plate format was developed and validated. A proof of concept for ADI engineering resulted in a pH optimum of pH 7.0 and increased resistance under physiological and slightly alkaline conditions. At pH 7.4, variant M2 (K5T/ D44E/H404R) is four times faster than the wild-type PpADI and retains -50% of its activity relative to its pH optimum, compared to -10% in the case of the wild-type PpADI.

L337H mutant of rat neuronal nitric oxide synthase resembles human neuronal nitric oxide synthase toward inhibitors

Fang, Jianguo,Ji, Haitao,Lawton, Graham R.,Xue, Fengtian,Roman, Linda J.,Silverman, Richard B.

, p. 4533 - 4537 (2009)

A common dichotomy exists in inhibitor design: should the compounds be designed to block the enzymes of animals in the preclinical studies or to inhibit the human enzyme? We report that a single mutation of Leu-337 in rat neuronal nitric oxide synthase (nNOS) to His makes the enzyme resemble human nNOS more than rat nNOS. We expect that the approach used in this study can unite the dichotomy and speed up the process of inhibitor design and development.

Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia

Li, Zhimin,Kulakova, Liudmila,Li, Ling,Galkin, Andrey,Zhao, Zhiming,Nash, Theodore E.,Mariano, Patrick S.,Herzberg, Osnat,Dunaway-Mariano, Debra

, p. 149 - 161 (2009)

Giardia lamblia arginine deiminase (GlAD), the topic of this paper, belongs to the hydrolase branch of the guanidine-modifying enzyme superfamily, whose members employ Cys-mediated nucleophilic catalysis to promote deimination of l-arginine and its naturally occurring derivatives. G. lamblia is the causative agent in the human disease giardiasis. The results of RNAi/antisense RNA gene-silencing studies reported herein indicate that GlAD is essential for G. lamblia trophozoite survival and thus, a potential target for the development of therapeutic agents for the treatment of giardiasis. The homodimeric recombinant protein was prepared in Escherichia coli for in-depth biochemical characterization. The 2-domain GlAD monomer consists of a N-terminal domain that shares an active site structure (depicted by an in silico model) and kinetic properties (determined by steady-state and transient state kinetic analysis) with its bacterial AD counterparts, and a C-terminal domain of unknown fold and function. GlAD was found to be active over a wide pH range and to accept l-arginine, l-arginine ethyl ester, Nα-benzoyl-l-arginine, and Nω-amino-l-arginine as substrates but not agmatine, l-homoarginine, Nα-benzoyl-l-arginine ethyl ester or a variety of arginine-containing peptides. The intermediacy of a Cys424-alkylthiouronium ion covalent enzyme adduct was demonstrated and the rate constants for formation (k1 = 80 s-1) and hydrolysis (k2 = 35 s-1) of the intermediate were determined. The comparatively lower value of the steady-state rate constant (kcat = 2.6 s-1), suggests that a step following citrulline formation is rate-limiting. Inhibition of GlAD using Cys directed agents was briefly explored. S-Nitroso-l-homocysteine was shown to be an active site directed, irreversible inhibitor whereas Nω-cyano-l-arginine did not inhibit GlAD but instead proved to be an active site directed, irreversible inhibitor of the Bacillus cereus AD.

Ruthenium(III) readily abstracts NO from L-arginine, the physiological precursor to NO, in the presence of H2O2. A remarkably simple model system for NO synthases.

Marmion,Murphy,Nolan

, p. 1870 - 1871 (2001)

Reaction of [Ru(Hedta)Cl]- with H2O2 in the presence of arginine, produces NO, in the form of an Ru(II)-(NO+) complex and citrulline which is a remarkably simple model system for the physiological NO synthase reaction.

IMPROVED METHOD OF SYNTHESIS AND PURIFICATION OF CITRULLINE

-

Paragraph 00033-00034; 00037-00038, (2020/12/29)

This invention provides for synthesis of citrulline from a transition metal complex of ornithine using cyanate to derivatize the terminal amino group of ornithine. The invention also provides improved methods for purification of citrulline produced by reaction of cyanate with ornithine via the steps of reprecipitation of copper complex of citrulline, removal of the complexing metal by sulfide precipitation, activated carbon adsorption and antisolvent crystallization.

l-Arginine and nitric oxide synthesis in the cells with inducible NO synthase

Kuropteva,Baider,Nagler,Bogatyrenko,Belaia

, p. 174 - 180 (2019/04/25)

The effect of citrulline and ammonium chloride on the nitric oxide formation by peritoneal macrophages and liver tissue cells was studied using ESR spectroscopy. In ex vivo models, the incubation of cells capable of expressing inducible NO synthase (iNOS) with interferon-γ resulted in a moderate increase in the amount of hemoglobin–nitric oxide nitrosyl complexes (Heme–NO NCs), whereas incubation with l-citrulline and ammonium chloride increased the amount of Heme–NO NCs by an order of magnitude. It was assumed that a separate cycle of L-arginine and nitric oxide synthesis exists in the peritoneal macrophages and liver cells, with the major participants of the cycle being the inducible NO synthase enzyme (iNOS) and enzymes that synthesize L-arginine from L-citrulline and a nitrogen source. Functioning of this cycle makes immunocompetent cells with iNOS able to produce NO for a long time and in large amounts.

Enzyme-immobilized metal-organic framework nanosheets as tandem catalysts for the generation of nitric oxide

Gao, Feng,Lei, Jianping,Ling, Pinghua,Qian, Caihua

supporting information, p. 11176 - 11179 (2020/04/23)

An enzyme-immobilized metal-organic framework (MOF) nanosheet system was developed as a tandem catalyst, which converted glucose into gluconic acid and H2O2, and sequentially the latter could be used to catalyze the oxidation of l-arginine to generate nitric oxide in the presence of porphyrinic MOFs as artificial enzymes under physiological pH, showing great potential in cancer depleting glucose for starving-like/gas therapy.

Method for preparing L-citrulline crude product and L-citrulline prepared through method

-

Paragraph 0033-0108, (2017/05/05)

The invention discloses a method for preparing an L-citrulline crude product and L-citrulline prepared through the method. The method for preparing the L-citrulline crude product includes the steps of preparing L-citrulline liquid, preparing the L-citrulline crude product from the L-citrulline liquid, refining the crude product, and obtaining an L-citrulline finished product. When the method is used for producing the L-citrulline crude product, no ethyl alcohol is used, so the method has the advantages that production conditions are mild, concentration time is short, product purity is high, yield is high and production cost is low.

Engineering nitric oxide synthase chimeras to function as NO dioxygenases

Wang, Zhi-Qiang,Haque, Mohammad Mahfuzul,Binder, Katherine,Sharma, Manisha,Wei, Chin-Chuan,Stuehr, Dennis J.

, p. 122 - 130 (2016/06/08)

Nitric oxide synthases (NOSs) catalyze a two-step oxidation of l-arginine to form nitric oxide (NO) and l-citrulline. NOS contains a N-terminal oxygenase domain (NOSoxy) that is the site of NO synthesis, and a C-terminal reductase domain (NOSred) that binds nicotinamide adenine dinucleotide phosphate (NADPH), flavin adenine dinucleotide (FAD), and flavin mononucleotide (FMN) and provides electrons to the NOSoxy heme during catalysis. The three NOS isoforms in mammals inducible NOS (iNOS), neuronal NOS (nNOS), and endothelial NOS (eNOS) share high structural similarity but differ in NO release rates and catalytic properties due to differences in enzyme kinetic parameters. These parameters must be balanced for NOS enzymes to release NO, rather than consume it in a competing, inherent NO dioxygenase reaction. To improve understanding, we drew on a global catalytic model and previous findings to design three NOS chimeras that may predominantly function as NO dioxygenases: iNOSoxy/nNOSred (Wild type (WT) chimera), V346I iNOSoxy/nNOSred (V346I chimera) and iNOSoxy/S1412D nNOSred (S1412D chimera). The WT and S1412D chimeras had higher NO release than the parent iNOS, while the V346I chimera exhibited much lower NO release, consistent with expectations. Measurements indicated that a greater NO dioxygenase activity was achieved, particularly in the V346I chimera, which dioxygenated an estimated two to four NO per NO that it released, while the other chimeras had nearly equivalent NO dioxygenase and NO release activities. Computer simulations of the global catalytic model using the measured kinetic parameters produced results that mimicked the measured outcomes, and this provided further insights on the catalytic behaviors of the chimeras and basis of their increased NO dioxygenase activities.

Process route upstream and downstream products

Process route

L-citrulline copper complex

L-citrulline copper complex

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With sodium sulfide; In water; Reagent/catalyst; Large scale;
Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
for 46 - 120h; Product distribution / selectivity; Enzymatic reaction;
91%
With dihydrogen peroxide; K[Ru(Hedta)Cl]*2H2O;
71%
durch Einwirkung von Faeulnisbakterien;
durch Einwirkung von Pseudomonas aeruginosa (Bacillus pyocyaneus);
durch Einwirkung von Streptococcus faecalis;
With recombinant neuronal nitric oxide synthase; Further Variations:; Reagents; Enzyme kinetics;
With arginine deiminase; potassium 2-(N-morpholino)ethanesulfonate; magnesium chloride; at 25 ℃; pH=5.6; Enzyme kinetics;
With neuronal nitric oxide synthase μ; NADPH; calmodulin; at 25 ℃; Further Variations:; Reaction partners; Reagents; pH-values; Enzyme kinetics;
With magnesium chloride; In various solvent(s); at 25 ℃; pH=5.6; Enzyme kinetics;
With glutamate dehydrogenase; 1,4-dihydronicotinamide adenine dinucleotide; In various solvent(s); at 25 ℃; pH=7.0; Enzyme kinetics;
With magnesium chloride; In various solvent(s); at 25 ℃; pH=5.6; Enzyme kinetics;
With magnesium chloride; In various solvent(s); at 25 ℃; pH=7.5; Enzyme kinetics;
With magnesium chloride; In various solvent(s); at 25 ℃; pH=6.0; Enzyme kinetics;
With full-length inducible nitric oxide synthase; (6R)-5,6,7,8-tetrahydro-L-biopterin; oxygen; at 37 ℃; pH=7.4; Kinetics; aq. buffer;
With 1,4-dithio-D,L-threitol; human neuronal nitric oxide synthase; NADPH; calcium chloride; hemoglobin; calmodulin; (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; at 20 ℃; pH=7.4; Concentration; Reagent/catalyst; Kinetics; aq. Hepes buffer; Enzymatic reaction;
With α-ketoglutaric acid; bovine liver glutamate dehydrogenase type II; recombinant Giardia lamblia arginine deiminase; water; at 25 ℃; pH=7.5; pH-value; Reagent/catalyst; Time; Kinetics; aq. buffer;
With arginine deiminase K5T/D44E/H404R mutant; at 37 ℃; Reagent/catalyst; pH-value; Kinetics; aq. phosphate buffer;
With 1,4-dithio-D,L-threitol; neuronal NO synthase; NADPH; FAD; 4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acid; (6-R,S)-5,6,7,8-tetrahydro-L-biopterin dihydrochloride; Flavin mononucleotide; superoxide dismutase; catalase; calmodulin; at 25 ℃; Enzymatic reaction;
With hydrogenchloride; water; at 38 ℃; for 96h; pH=6;
N-hydroxy-L-arginine

N-hydroxy-L-arginine

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With dihydrogen peroxide; Cl8TPPFe(III)Cl; In various solvent(s); at 20 ℃;
N<sup>ω</sup>-tert-butoxy-L-arginine

Nω-tert-butoxy-L-arginine

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With mammalian nitric oxide synthase; NADPH; diothiothreitol; tetrahydrobiopterin; In various solvent(s); at 30 ℃; for 0.0333333h; Enzyme kinetics;
N<sup>ω</sup>-O-(3-methyl-2-butenyl)hydroxy-L-arginine

Nω-O-(3-methyl-2-butenyl)hydroxy-L-arginine

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With mammalian nitric oxide synthase; NADPH; diothiothreitol; tetrahydrobiopterin; In various solvent(s); at 30 ℃; for 0.0333333h; Enzyme kinetics;
Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With copper (II) carbonate hydroxide; water; at 100 ℃; Durch Erhitzen des erhaeltlichen Komplexsalzes mit Harnstoff in wss. Loesung auf 100grad und Zerlegung des gebildeten Kupfer(II)-Komplexsalzes des L-Citrullins mit H2S in Wasser;
L-ornithine hydrochloride
3184-13-2,36630-89-4

L-ornithine hydrochloride

urea
57-13-6

urea

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
L-ornithine hydrochloride; With sodium hydrogencarbonate; In water; at 20 ℃;
With copper(ll) sulfate pentahydrate; In water; at 100 ℃;
urea; Further stages;
Conditions
Conditions Yield
With carbamoyl phosphate;
Citrulline
372-75-8

Citrulline

nitrogen(II) oxide
10102-43-9

nitrogen(II) oxide

Conditions
Conditions Yield
With inducible NO synthase; at 20 ℃; Enzymatic reaction;
With dihydrogen peroxide; C48H28ClFeN4O8; In aq. phosphate buffer; for 0.416667h; pH=7.4; Kinetics; Green chemistry;
Nω-allyl-L-arginine
139461-37-3

Nω-allyl-L-arginine

Citrulline
372-75-8

Citrulline

Conditions
Conditions Yield
With NADPH; calcium chloride; calmodulin; neuronal nitric oxide synthase; at 20 ℃; pH=7.5; Enzyme kinetics; Enzymatic reaction;

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