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Merck
모든 사진(1)

주요 문서

A4021

Sigma-Aldrich

Nε-Acetyl-L-lysine

≥98% (TLC)

동의어(들):

N6-acetyl-L-lysine

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About This Item

Linear Formula:
CH3CONH(CH2)4CH(NH2)CO2H
CAS Number:
Molecular Weight:
188.22
EC Number:
MDL number:
UNSPSC 코드:
12352209
PubChem Substance ID:
NACRES:
NA.26

제품명

Nε-Acetyl-L-lysine,

분석

≥98% (TLC)

Quality Level

양식

powder

농도

50 mg/mL in 80% acetic acid

색상

colorless to white

mp

250 °C (dec.) (lit.)

저장 온도

−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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애플리케이션


  • 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).

생화학적/생리학적 작용

Nε-Acetyl-L-lysine (L-AcK) is an R-chain N-acetylated α amino acid used together with other lysine analogues to differentiate and characterized various aminoacylases and regulator 2 (Sir2) enzymes/sirtuins.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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시험 성적서(COA)

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문서 라이브러리 방문

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
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
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.

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