AcdK 

AcdK is a non-natural amino acid and a precursor of allysine. AcdK allows site-specific incorporation into target proteins in E. coli via the amber suppression strategy. AcdK enables site-specific lysine dimethylation or monomethylation modification of target proteins. AcdK can synthesize site-specific lysine-methylated variants of histone H3 and p53, which is applicable for investigating the substrate specificity and catalytic function of epigenetic enzymes^[1].

AcdK (0.5 mM) is efficiently and site-specifically incorporated into sfGFP at position D134 in E. coli BL21(DE3) cells, and subsequent biocompatible reactions enable quantitative conversion to sfGFP with site-specific lysine dimethylation at position D134^[1].
AcdK (2 mM) is efficiently and site-specifically incorporated into histone H3 at positions K4, K9, or K36 in E. coli BL21(DE3) cells, and subsequent biocompatible reactions enable conversion to site-specific dimethylated histone H3 variants^[1].
AcdK is efficiently and site-specifically incorporated into p53 at position K372 in E. coli BL21(DE3) cells, and subsequent biocompatible reactions enable conversion to p53 with site-specific lysine mono- or dimethylation at K372, which directly enhances Tip60-catalyzed acetylation of p53 at K120 by 2.5- to 3-fold^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

319.32

C₁₄H₁₇N₅O₄

2097535-26-5

OC([C@@H](N)CC/C=C/NC(OCC1=CC=C(C=C1)N=[N+]=[N-])=O)=O

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Wang ZA, et al. A Genetically Encoded Allysine for the Synthesis of Proteins with Site-Specific Lysine Dimethylation. Angew Chem Int Ed Engl. 2017;56(1):212-216.  [Content Brief]