12685
Nω-磷酸-L-精氨酸 锂盐 水合物
≥95.0% (TLC)
别名:
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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关于此项目
经验公式（希尔记法）:
C6H15N4O5P · xLi+ · yH2O
化学文摘社编号:
分子量:
254.18 (free acid basis)
UNSPSC Code:
12352209
NACRES:
NA.26
EC Number:
214-714-7
InChI key
CCTIOCVIZPCTGO-BYPYZUCNSA-N
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
assay
≥95.0% (TLC)
form
powder or crystals
color
white to off-white
storage temp.
−20°C
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
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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
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
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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