推荐产品
产品名称
Nε-乙酰基- L -赖氨酸,
方案
≥98% (TLC)
质量水平
表单
powder
浓度
50 mg/mL in 80% acetic acid
颜色
colorless to white
mp
250 °C (dec.) (lit.)
储存温度
−20°C
SMILES字符串
CC(=O)NCCCC[C@H](N)C(O)=O
InChI
1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13)/t7-/m0/s1
InChI key
DTERQYGMUDWYAZ-ZETCQYMHSA-N
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应用
- Nε-Acetyl L-α Lysine Improves Activity and Stability of α-Amylase at Acidic Conditions: A Comparative Study with other Osmolytes. This study highlights the use of Nε-Acetyl-ʟ-lysine in enhancing the functional stability and activity of α-amylase under acidic conditions, demonstrating its potential as a valuable additive in industrial enzyme applications (Joghee et al., 2020).
生化/生理作用
Nε-乙酰基-L-赖氨酸 (L-AcK) 是一种 R 链 N-乙酰化 α氨基酸与其他赖氨酸类似物一起用于区分和表征各种氨基酰化酶和调节因子 2 (Sir2) 酶/去乙酰化酶。
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Nature chemical biology, 4(4), 232-234 (2008-02-19)
N(epsilon)-acetylation of lysine (1) is a reversible post-translational modification with a regulatory role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize proteins containing N(epsilon)-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of
Zeitschrift fur Lebensmittel-Untersuchung und -Forschung, 198(1), 66-67 (1994-01-01)
After heating N alpha-acetyllysine and glucose for 4 h at 90 degrees C in the dry state and subsequent acid hydrolysis with 7.8 N HCl, preparative fractionation of the dihydrochlorides of furosine and pyridosine was achieved by cation-exchange chromatography. The
Chemical research in toxicology, 11(9), 995-1004 (1998-10-07)
Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both Nepsilon-(dichloroacetyl)-L-lysine and Nepsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis.
Journal of the American Chemical Society, 132(35), 12286-12298 (2010-08-20)
Sirtuins are protein-modifying enzymes distributed throughout all forms of life. These enzymes bind NAD(+), a universal metabolite, and react it with acetyllysine residues to effect deacetylation of protein side chains. This NAD(+)-dependent deacetylation reaction has been observed for sirtuin enzymes
The Journal of biological chemistry, 273(9), 4997-5005 (1998-03-28)
We have recently demonstrated that neutrophils oxidize nearly all of the amino acids commonly found in plasma to a corresponding family of aldehydes in high yield. The reaction is mediated by hypochlorous acid (HOCl), the major oxidant generated by the
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