Lysine bound

Histone Acetylation. Figure 1 Histone acetylation is a posttranslational modification of lysine residues of histones. This modification is catalyzed by histone actyl transferases (HATs), which transfer an acetyl group (yellow) from acetyl-Coenzyme A onto the E-amino group of the lysine residue. Histone deacetylation is catalyzed by histone deacetylases (HDACs), which hydrolyze the lysine bound acetyl group. HDAC inhibitors like Trichostatin A (TSA) are known to inhibit the deacetylation reaction in vivo and in vitro. 

Most recently, Baltzer and co-workers have incorporated a lysine-bound nicotinamide into a more complex peptide scaffold [75]. This approach takes advantage of the augmented reactivity of a lysine residue contained in a helix-turn-helix scaffold (as described previously [76]). An adjacent histidine is able to selectively catalyze the formation of an amide bond between activated esters and the lysine c-amino group under aqueous conditions. Thus, reaction of the 42-residue peptide LA-42 withp-nitrophenyl hT-methylnicotinate in an aqueous solution at pH 5.9 yields the nicotinoyl-functionalized peptide (Fig. 27). 

Metabolic Transit of Lysine Bound to Caffeic Acid. In order to follow the metabolism of lysine bound to caffeic acid, goat casein, biologically labelled with tritiated lysine, was treated with caffeic acid at pH 7 with tyrosinase and at pH 10 without tyrosinase and was given to rats. The urinary and fecal excretions and the incorporation of lysine in the tissues were measured (120) (see Figure 6). 

Schleicher E, Wieland OH. Specific quantitation by HPLC of protein (lysine) bound glucose in human serum albumin and other glycosylated proteins. 

Schleicher, E., and Wieland, O. H., Specific quantitation by HPLC of protein (lysine) bound glucose in human. serum albumin and other glycosylated proteins. J. Clin. Chem. Clin. Biochem. 19, 81-87 (1981). 

V8. Vogt, B. W, Schleicher, E. D., and Wieland, O. H., e-Amino-lysine-bound glucose in human tissues obtained at autopsy. Increase in diabetes mellitus. Diabetes 31, 1123-1127 (1982). 

In nature, lysine-bound lipoic acid is used to oxidize thiamine-bound acetyldehyde to acetic acid. The reduced dithiol is then reoxidized to the disulfide by a flavin. The lysine oligomethylene chain is thought to act as a pendulum string, when lipoic swings back and forth betwen thiamine and flavin coenzymes... 

Figure 11.16. Anisotropy decay ofdansyl-lysine bound to the antigen binding sites of IgE in the absence and in the presence of the membrane receptor. Revised and reprinted, with permission, firom Ref, 74, Copyright 1990, American Chemical Sodeiy.

L-lysine bound to agarose on the affinity of rabbit plasminogen for the matrix... 

Passive, no competition with lysine" " bound to protein little absorption (< 10%) Slowly absorbed, not metabolised" ... 

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