The word "PPIase" is a shortened form of "peptidyl-prolyl cis-trans isomerase," an enzyme that catalyzes the isomerization of peptide bonds. Its spelling is derived from the acronym PPI, which stands for peptidyl-prolyl isomerase. The "ase" suffix is added to denote that it is an enzyme. In IPA phonetic transcription, it is pronounced as /pi pi aɪs/, with emphasis on the first syllable and a long "i" sound. The correct spelling and pronunciation of this word are important in scientific research and literature.
PPIase, also known as peptidyl-prolyl cis-trans isomerase, refers to a class of enzymes that catalyze the interconversion of the cis and trans isomers of proline peptide bonds in proteins. The term PPIase stands for peptidyl-prolyl isomerase, where the prefix "peptidyl" signifies that the enzyme acts on the peptide chains, "prolyl" relates to its specificity for proline residues, and "isomerase" implies its role in catalyzing isomerization reactions.
PPIases play a crucial role in protein folding and conformational changes, as the cis and trans isomeric forms of proline residues can adopt distinct protein conformations. By catalyzing the conversion between these isomers, PPIases assist in enhancing the efficiency of protein folding, stability, and biological activity. These enzymes are found ubiquitously in nature, with different Isoforms and families identified across various organisms.
PPIases can be classified into three main families based on their structural and functional characteristics: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. Cyclophilins are primarily targeted by cyclosporine A, a potent immunosuppressive drug, whereas FKBPs are modulated by FK506 and rapamycin. Parvulins, on the other hand, exhibit a different structural fold compared to cyclophilins and FKBPs.
Due to their involvement in critical cellular processes, dysregulation or malfunctioning of PPIases has been correlated with various diseases, including neurodegenerative disorders, cancer, and autoimmune conditions. Therefore, studying PPIases and their inhibitors has gained significant attention in drug development
The word "PPIase" is an abbreviation for "peptidyl-prolyl cis-trans isomerase". The etymology of this word can be broken down as follows:
1. Peptidyl: Derived from "peptide", referring to a short chain of amino acids joined together by peptide bonds.
2. Prolyl: Derived from "proline", which is an amino acid with a unique structure that affects protein conformation and function.
3. Cis-trans: Indicates the isomerization process, where a peptidyl-prolyl bond can undergo a conformational change from cis (same side) to trans (opposite side) or vice versa.
4. Isomerase: Derived from "isomer", which refers to compounds with the same molecular formula but different structural arrangement. An isomerase is an enzyme that facilitates the interconversion of isomers.