产品名称
Nε-乙酰基- L -赖氨酸,
InChI key
DTERQYGMUDWYAZ-ZETCQYMHSA-N
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
SMILES string
CC(=O)NCCCC[C@H](N)C(O)=O
assay
≥98% (TLC)
form
powder
concentration
50 mg/mL in 80% acetic acid
color
colorless to white
mp
250 °C (dec.) (lit.)
storage temp.
−20°C
Quality Level
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Application
- Nε-乙酰基L-α赖氨酸在酸性条件下提高α-淀粉酶的活性和稳定性与其它渗透物的比较研究。该研究强调了Nε-乙酰基-L-赖氨酸在酸性条件下增强α-淀粉酶的功能稳定性和活性,证明了其作为工业酶应用中有价值的添加剂的潜力(Joghee et al., 2020)。
Biochem/physiol Actions
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。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Heinz Neumann et al.
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
T Henle et al.
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
A Pähler et al.
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.
Jarrod B French et al.
Biochemistry, 47(38), 10227-10239 (2008-08-30)
Sirtuins are NAD (+)-dependent enzymes that deacetylate a variety of cellular proteins and in some cases catalyze protein ADP-ribosyl transfer. The catalytic mechanism of deacetylation is proposed to involve an ADPR-peptidylimidate, whereas the mechanism of ADP-ribosyl transfer to proteins is
Yana Cen et al.
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
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