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Eupeptide bond

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Definition

noun, plural: eupeptide bonds

A peptide bond characterized by forming a link between the C-1 (alpha-carboxyl group) of one amino acid to the N-2 of another amino acid


Supplement


A eupeptide bond is the predominant type of peptide bond. The term is used in contrast to another type of peptide bond, isopeptide bond. In eupeptide bond, the peptide bond forms between the carbon 1 of alpha-amino acid and nitrogen 2 of another amino acid. In contrast, the isopeptide bond forms between the between the carboxyl group and an amino group of joining amino acids where at least one of them is part of the side chain.

A eupetide bond, or simply peptide bond, joins amino acids with a concomitant release of water molecule. Thus, the process is a type of dehydration synthesis reaction. Water is formed when, for instance, two amino acids are joining together, one loses a hydrogen and oxygen from the carboxyl group while the other loses a hydrogen from the amine group.

Series of amino acids joined together make up a peptide. A peptide is one of the major biomolecules. Peptides may be classified based on the number of their monomeric units. For instance, a dipeptide is a peptide made up of two amino acids whereas a tripeptide is a peptide consisting of three amino acids. A polypeptide is a peptide made up of longer chain of amino acids.

The eupeptide bond is the more predominant type than the isopeptide bond. This form of chemical bond can be degraded through the process of hydrolysis, i.e. the addition of water. In living systems, the process may take place by using enzymes.


Word origin: eu- (true) + -peptide

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