isopeptide bond


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i·so·pep·tide bond

an amide linkage between a carboxyl group of one amino acid and an amino group of another amino acid in which at least one of these groups is not on the α-carbon of one of the amino acids; for example, the bond between the glutamyl residue and the cysteinyl residue of glutathione. Compare: peptide bond, eupeptide bond.
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Structurally, ubiquitin is an 8.5 kDa, 76 amino acid polypeptide that forms a compact structure with an exposed carboxy terminal tail containing a diglycine motif that can be covalently ligated via an isopeptide bond to the primary e-amino group of lysine (Lys) residues on a target substrate.
Ubiquitination of neurotransmitter receptors and postsynaptic scaffolding proteins
Its insolubility is largely attributable to cross-linking of certain structural proteins by a series of transglutaminase (TGase) enzymes which form an [N.sup.[Epsilon]]([Gamma]-glutamyl) lysine isopeptide bond between the [Gamma]-amide sidechain of a donor glutamine residue and the [Epsilon]-N[H.sub.2] sidechain group of an acceptor lysine residue.
Structural-mechanical integration of keratin intermediate filaments with cell peripheral structures in the cornified epidermal keratinocyte
FXIIIa is a transglutaminase that catalyzes the formation of isopeptide bonds between the free amine group of a lysine residue and the acyl group at the end of the side chain of a glutamine residue [1].
Inhibition of Fibrinolysis by Coagulation Factor XIII
He noted that aging slows ubiquitin-proteasome proteolytic activity, resulting in the accumulation of ubiquitinylated proteins via isopeptide bonds. This accumulation causes the onset of inflammation.
An industry bubbling with new ideas: SODEOPEC looks at the latest developments that are impacting the detergent and personal care industry
As you may know, transglutaminase is a transferase that forms isopeptide bonds between lysyl and glutaminyl residues.
Modify whey protein's rheological properties using immobilized enzyme
It is possible that the EDTA-insensitive [[alpha].sub.2]M is covalently linked via transglutaminase-catalyzed isopeptide bonds. The Limulus clot does contain such protein-protein bonds [12] and human [[alpha].sub.2]M is a substrate for transglutaminase crosslinking.
Association of [[alpha].sub.2]-Macroglobulin with the Coagulin Clot in the American Horseshoe Crab, Limulus polyphemus: A Potential Role in Stabilization from Proteolysis
Thiol ester activation hydrolyses this bond, releasing the [gamma]-carbonyl of Gln, which in LAM establishes isopeptide bonds with the [epsilon]-amino group of Lys-254 (3), and the thiol of Cys.
Potentiation of limulin-mediated cytolysis by thiol ester-reacted forms of limulus alpha2-macroglobulin: identification of functionally important domains

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