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12685

Sigma-Aldrich

Nω-Phospho-L-arginine lithium salt hydrate

≥95.0% (TLC)

Synonym(s):

H-Arg(PO3H2)-OH lithium salt, N5-(Phosphonoamidino)-L-ornithine lithium salt, N5-[Imino(phosphonoamino)methyl]-L-ornithine lithium salt, L-2-Amino-5-(N′-phosphonoguanidino)valeric acid lithium salt, Lithium L-arginine phosphate

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About This Item

Empirical Formula (Hill Notation):
C6H15N4O5P · xLi+ · yH2O
CAS Number:
Molecular Weight:
254.18 (free acid basis)
EC Number:
UNSPSC Code:
12352209
NACRES:
NA.26

Assay

≥95.0% (TLC)

form

powder or crystals

color

white to off-white

storage temp.

−20°C

InChI

1S/C6H15N4O5P/c7-4(5(11)12)2-1-3-9-6(8)10-16(13,14)15/h4H,1-3,7H2,(H,11,12)(H5,8,9,10,13,14,15)/t4-/m0/s1

InChI key

CCTIOCVIZPCTGO-BYPYZUCNSA-N

Biochem/physiol Actions

Important metabolite in arginine and proline metabolism, high-energy metabolite, constituent of crustaceans and crayfish muscle.

Analysis Note

may contain 8% more water then theoretically in monohydrate expected

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Omar Davulcu et al.
Biochemistry, 50(19), 4011-4018 (2011-03-24)
Arginine kinase catalyzes the reversible transfer of a phosphoryl group between ATP and arginine. It is the arthropod homologue of creatine kinase, buffering cellular ATP levels. Crystal structures of arginine kinase, in substrate-free and substrate-bound forms, have revealed large conformational
Gaspar E Canepa et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 160(1), 40-43 (2011-06-01)
Phytomonas are trypanosomatid plant parasites closely related to parasites that cause several human diseases. Little is known about the biology of these organisms including aspects of their metabolism. Arginine kinase (E.C. 2.7.3.3) is a phosphotransferase which catalyzes the interconversion between
Karina D García-Orozco et al.
International archives of allergy and immunology, 144(1), 23-28 (2007-05-15)
Consumption of seafood can produce allergic symptoms in susceptible individuals and crustacean allergies are the most frequently reported causes of allergic reactions. An allergen from the muscle of the white shrimp Litopenaeus vannamei was purified by ion exchange chromatography and
Jonathan Bragg et al.
Journal of bacteriology, 194(10), 2668-2676 (2012-03-06)
Arginine kinases catalyze the reversible transfer of a high-energy phosphoryl group from ATP to l-arginine to form phosphoarginine, which is used as an energy buffer in insects, crustaceans, and some unicellular organisms. It plays an analogous role to that of
Margaret Werr et al.
Insect biochemistry and molecular biology, 39(9), 634-645 (2009-07-15)
Arginine kinase (ATP:l-arginine omega-N-phosphotransferase, EC2.7.3.3.; AK) is an enzyme crucial for the energy metabolism of insects and other invertebrates, that has known allergenic potential in humans and that has been proposed as a pesticidal drug target. Here we report the

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