Peptide Bond
A Peptide Bond is a molecular bond that links 2 consecutive amino acid monomers along a peptide or protein chain.
- AKA: Amide Bond.
- …
- Counter-Example(s):
- See: Peptide, Chemical Bond, Amino Acid.
References
2017
- (Wikipedia, 2017) ⇒ https://en.wikipedia.org/wiki/Peptide_bond Retrieved:2017-7-9.
- A peptide bond (amide bond) is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain.[1] [2] [3] [4] [5]
Synthesis
When two amino acids form a dipeptide through a peptide bond it is called condensation. In condensation, two amino acids approach each other, with the acid moiety of one coming near the amino moiety of the other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (-CO-NH-). The two joined amino acids are called a dipeptide.
The peptide bond is synthesized when the carboxyl group of one amino acid molecule reacts with the amino group of the other amino acid molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction).
The formation of the peptide bond consumes energy, which, in living systems, is derived from ATP.[6] Polypeptides and proteins are chains of amino acids held together by peptide bonds. Living organisms employ enzymes to produce polypeptides, and ribosomes to produce proteins. Peptides are synthesized by specific enzymes. For example, the tripeptide glutathione is synthesized in two steps from free amino acids, by two enzymes: gamma-glutamylcysteine synthetase and glutathione synthetase.[7][8]
- A peptide bond (amide bond) is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain.[1] [2] [3] [4] [5]
- ↑ Walker, CBE FRSE, Peter M. B., ed. (1990) [1988]. Cambridge Dictionary of Science and Technology (reprint ed.). Edinburgh: Press Syndicate of the University of Cambridge. p. 658. ISBN 0521394414.
- ↑ Pauling L. (1960) The Nature of the Chemical Bond, 3rd. ed., Cornell University Press.
- ↑ Stein RL. (1993) "Mechanism of Enzymatic and Nonenzymatic Prolyl cis-trans Isomerization", Adv. Protein Chem., 44, 1–24.
- ↑ Schmid FX, Mayr LM, Mücke M and Schönbrunner ER. (1993) "Prolyl Isomerases: Role in Protein Folding", Adv. Protein Chem., 44, 25–66.
- ↑ Fischer G. (1993) "Peptidyl-Prolyl cis/trans Isomerases and Their Effectors", Angew. Chem. Int. Ed. Engl., 33, 1415–1436.
- ↑ Watson, James; Hopkins, Nancy; Roberts, Jeffrey; Agetsinger Steitz, Joan; Weiner, Alan (1987) [1965]. Molecualar Biology of the Gene (hardcover) (Fourth ed.). Menlo Park, CA: The Benjamin/Cummings Publishing Company, Inc.. p. 168. ISBN 0805396144.
- ↑ "Glutathione metabolism and its implications for health". The Journal of Nutrition 134 (3): 489–92. March 2004. PMID 14988435. http://jn.nutrition.org/cgi/pmidlookup?view=long&pmid=14988435.
- ↑ Meister A (November 1988). "Glutathione metabolism and its selective modification". The Journal of Biological Chemistry 263 (33): 17205–8. PMID 3053703. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3053703.