Merck
CN

A4021

Sigma-Aldrich

Nε-乙酰基- L -赖氨酸

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别名:
N6-acetyl-L-lysine
线性分子式:
CH3CONH(CH2)4CH(NH2)CO2H
CAS号:
分子量:
188.22
EC 号:
MDL编号:
PubChem化学物质编号:
NACRES:
NA.26

检测方案

≥98% (TLC)

形式

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 string

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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相关类别

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


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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
S L Hazen et al.
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
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
J A Cohn et al.
Archives of biochemistry and biophysics, 328(1), 158-164 (1996-04-01)
We have previously shown that incubation of the model protein glucose-6-phosphate dehydrogenase (Glu-6-PDH) from the bacterium Leuconostoc mesenteroides with 4-hydroxy-2-nonenal (HNE), a major product of lipid peroxidation, results in the formation of cross-linked protein. HNE-modified protein is resistant to proteolytic
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

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