Lysyl residues

Trypsin-like proteinases are serine proteinases that recognized peptide residues with positively charged side chains (arginyl or lysyl residues) and that effect... 

Collagen triple helices are stabilized by hydrogen bonds between residues in dijferent polypeptide chains. The hydroxyl groups of hydroxyprolyl residues also participate in interchain hydrogen bonding. Additional stability is provided by covalent cross-links formed between modified lysyl residues both within and between polypeptide chains. 

Figure29-1. Partial reactions in the attachment of ubiquitin (UB) to proteins. (1) The terminal COOH of ubiquitin forms a thioester bond with an -SH of E, in a reaction driven by conversion of ATP to AMP and PP. Subsequent hydrolysis of PP by pyrophosphatase ensures that reaction 1 will proceed readily. (2) A thioester exchange reaction transfers activated ubiquitin to Ej. (3) E3 catalyzes transfer of ubiquitin to e-amino groups of lysyl residues of target proteins.

Hydroxylation of prolyl residues and some lysyl residues glycosylation of some hydroxylysyl residues... 

After secretion from the cell, certain lysyl residues of tropoelastin are oxidatively deaminated to aldehydes by lysyl oxidase, the same enzyme involved in this process in collagen. However, the major cross-links formed in elastin are the desmosines, which result from the condensation of three of these lysine-derived aldehydes with an unmodified lysine to form a tetrafunctional cross-hnk unique to elastin. Once cross-linked in its mature, extracellular form, elastin is highly insoluble and extremely stable and has a very low turnover rate. Elastin exhibits a variety of random coil conformations that permit the protein to stretch and subsequently recoil during the performance of its physiologic functions. 

Figure 4. Cellulose acetate electrophoresis of hemoglobins. Variations in the quantities of Hb-Ag are hardly detectable (cornpare the samples 2 and 3 from top). Hb-N Baltimore is a p-chain variant in which lysyl residue in position 95 is replaced by a glutarnyl residue.

Graham DG, Anthony DC, Boekelheide K, et al. 1982. Studies of the molecular pathogenesis of hexane neuropathy. II. Evidence that pyrrole derivatization of lysyl residues leads to protein crosslinking. Toxicol Appl Pharmacol 64 415-422. 

This enzyme [EC 3.4.14.1], also called cathepsin C and cathepsin J, catalyzes the hydrolysis of a peptide bond resulting in the release of an N-terminal dipeptide, XaaXbb-Xcc, except when Xaa is an arginyl or a lysyl residue, or Xbb or Xcc is a prolyl residue. This enzyme, a member of the peptidase family Cl, is a CF-dependent lysosomal cysteine-type peptidase. 

This calcium-activated enzyme [EC 3.4.21.75] catalyzes the hydrolysis of peptide bonds in protein precursors that results in the release of mature proteins from their proproteins by hydrolysis of ArgXaaYaaArg—Zaa bonds, where Xaa can be any amino acid and Yaa is an arginyl or a lysyl residue. Albumin, complement component C3, and von Willebrand factor are thus released from their respective precursors. Furin is a member of the peptidase family S8. 

An acyl-transfer and redox coenzyme containing two sulfhydryl groups that form a dithiolane ring in the oxidized (disulfide) form. The redox potential at pH 7 is -0.29 volts. Lipoic acid is attached to the e-amino group of lysyl residues of transacetylases (subunit of a-ketoacid dehydrogenase complexes), thereby permitting acyl... 

This enzyme [EC 1.14.11.4] catalyzes the reaction of a procoUagen L-lysyl residue with a-ketoglutarate (or, 2-... 

This serine-protease [EC 3.4.21.87] catalyzes the hydrolysis of peptide bonds at Xaa—Yaa in which there is a preference for arginyl or lysyl residues at Xaa and Yaa. 

These enzymes [EC 6.3.2.19] catalyze the reaction of ATP with ubiquitin and a lysyl residue in a protein to produce a protein containing an iV-ubiquityllysyl residue, AMP, and pyrophosphate (or, diphosphate). Ubiquitin is coupled to the protein by an isopeptide bond between the C-terminal glycine of ubiquitin and -amino groups of lysyl residues in the protein. An intermediate in the reaction contains one ubiquitin residue bound as a thi-olester to the enzyme, and a residue of ubiquitin adenylate noncovalently bound to the enzyme. 

KINETIC ISOTOPE EFFECT LYSYL ENDOPEPTIDASE LYSYL HYDROXYLASE LYSYL OXIDASE Lysyl residue,... 

Systematic modification of the octapeptide sequence from cin-giotensinogen (Figure 1) was undertaken to incorporate desirable properties into the peptide. Addition of a prolyl residue to the N-termlnus Improved solubility at physiologic pH, replacement of the leucyl-leucine sequence with phenylalanyl residues Improved inhibitory properties by forty-fold, and addition of a lysyl residue to the C-termlnus Increased solubility and extended half-life in vivo. These modifications yielded the Renin Inhibitory Peptide TriP) vdiich effectively blocks renin both in primates (11) and man (1 2). 

Fig. 2. Kinetics of cross-linking of chondroitin 6-sulfate, a glycosaminoglycan (GAG), to collagen following exposure to 105 °C under 6.7 Pa (50 mtorr). The mechanism of cross-linking is most probably interchain amide condensation involving e-amino groups of lysyl residues on collagen chains with carboxylic groups on glucuronic acid residues in neighboring GAG chains (From [30] with permission).

Used for modifying -amino functions of lysyl residues in proteins [Bagree et al. FEBS LETT 120 275 1980. ... 

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