The word "prolyl isomerase" refers to an enzyme that catalyzes the isomerization of proline residues in proteins. Its spelling is derived from the two terms "prolyl" and "isomerase" which are pronounced as [ˈpɹoʊ.ləl] and [aɪˈsɒ.mə.reɪz], respectively. The IPA phonetic transcription of the word is [ˈpɹoʊ.ləl‿aɪˈsɒ.mə.reɪz], where the stress falls on the first syllable of "prolyl" and the second syllable of "isomerase". Getting the spelling right is important to understand the function and properties of this enzyme.
Prolyl isomerase, also known as peptidyl-prolyl cis-trans isomerase (PPIase), is an enzyme that catalyzes the cis-trans isomerization of prolyl peptide bonds in proteins. It specifically targets proline residues, which have a unique cyclic structure in the protein backbone. The cis and trans conformations of the proline residue differ in their spatial orientation, which can affect the folding, stability, and function of the protein.
Prolyl isomerases play a crucial role in protein folding and conformational changes, as proline residues are known to introduce strain into the protein structure. By catalyzing the cis-trans isomerization of proline bonds, prolyl isomerases can accelerate the folding process, promoting the acquisition of the correct protein conformation. They can also regulate protein function by facilitating conformational changes in response to various cellular signals or environmental conditions.
Prolyl isomerases are widely distributed in all domains of life, including bacteria, archaea, and eukaryotes. They are classified into different families based on their amino acid sequence and structural features. Some well-known examples include cyclophilins, parvulins, and FK506-binding proteins (FKBPs).
The discovery and characterization of prolyl isomerases have revealed their essential role in various cellular processes, such as protein trafficking, signal transduction, protein degradation, and immune response. Inhibition or dysregulation of prolyl isomerases has been implicated in several human diseases, including cancer, neurodegenerative disorders, and viral infections, making them potential therapeutic targets for drug development.
The word "Prolyl Isomerase" is composed of two main parts: "Prolyl" and "Isomerase".
"Prolyl" is derived from the amino acid "proline", which is one of the 20 standard amino acids found in proteins. The term "proline" comes from the Greek word "prolos", meaning "before" or "in front of". It was named by Richard Willstätter and his student Gleb Anrep in 1901.
"Isomerase" is a compound word consisting of the prefix "iso-" and the root word "merase". The prefix "iso-" is derived from the Greek word "isos", meaning "equal" or "same". It is commonly used to indicate isomers, which are compounds with the same molecular formula but different structural arrangements.