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Isopeptide bond between lysine and aspartate/asparagine. An isopeptide bond is a type of amide bond formed between a carboxyl group of one amino acid and an amino group of another. An isopeptide bond is the linkage between the side chain amino or carboxyl group of one amino acid to the α-carboxyl, α-amino group, or the side chain of another ...
Autocatalytic cycle of formose reaction showing how glyceraldehyde can be both the catalyst and the product of one portion of this complex reaction type. An early example of autocatalysis is the formose reaction , in which formaldehyde and base produce sugars and related polyols.
Bonds formed by transglutaminase exhibit high resistance to proteolytic degradation (proteolysis). [2] The reaction is [1] Gln-(C=O)NH 2 + NH 2-Lys → Gln-(C=O)NH-Lys + NH 3. Transglutaminases can also join a primary amine ( RNH 2 ) to the side chain carboxyamide group of a protein/peptide bound glutamine residue thus forming an isopeptide ...
Splicing of group I introns is processed by two sequential transesterification reactions. [3] First an exogenous guanosine or guanosine nucleotide (exoG) docks onto the active G-binding site located in P7, and then its 3'-OH is aligned to attack the phosphodiester bond at the "upstream" (closer to the 5' end) splice site located in P1, resulting in a free 3'-OH group at the upstream exon and ...
Autocatalytic sets were originally and most concretely defined in terms of molecular entities, but have more recently been metaphorically extended to the study of systems in sociology, ecology, and economics. Autocatalytic sets also have the ability to replicate themselves if they are split apart into two physically separated spaces.
A first kinetically controlled product rearranges to form the amide bond. The most common form of native chemical ligation uses a peptide thioester that reacts with a terminal cysteine residue. [58] Other methods applicable for covalently linking polypeptides in aqueous solution include the use of split inteins, [59] spontaneous isopeptide bond ...
The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl). [2]
The final step in the first ubiquitylation event is an attack from the target protein lysine amine group, which will remove the cysteine, and form a stable isopeptide bond. [6] One notable exception to this is p21 protein, which appears to be ubiquitylated using its N-terminal amine, thus forming a peptide bond with ubiquitin. [7]