How Do You Spell PEPTIDYLPROLYL ISOMERASE?

Pronunciation: [pˈɛptɪdˌɪlpɹəlˌɪl ˈa͡ɪsə͡ʊmɹˌe͡ɪz] (IPA)

Peptidylprolyl Isomerase is a pharmaceutical term that refers to a family of enzymes that catalyze the cis-trans isomerization of proline imidic peptide bonds in proteins. The correct spelling of this word is [pɛptɪdɪlproʊlɪlaɪsəmeɹeɪs]. The first syllable is "peptide," pronounced with a short "e" sound. The second syllable is "dil," pronounced with a long "i" sound. The third syllable is "prolyl," pronounced with a long "o" sound. The fourth syllable is "iso," pronounced with a long "i" sound. The final syllable is "merase," pronounced with a stress on the first syllable and a long "a" sound.

Meaning and Definition
Common Misspellings
Etymology
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PEPTIDYLPROLYL ISOMERASE Meaning and Definition

  1. Peptidylprolyl isomerase (PPIase) is an enzyme that catalyzes the isomerization of peptide bonds involving proline residues in proteins. Proline is known for its special structural properties, as its side chain forms a cyclic structure that imposes constraints on the backbone conformation of polypeptides. These constraints make proline residues prone to adopting the cis-conformation in peptide bonds, which can have significant effects on protein folding, stability, and function.

    Peptidylprolyl isomerases play a crucial role in modulating protein conformational changes, as they catalyze the interconversion between cis and trans isomers of proline residues. By facilitating the cis-trans isomerization, PPIases contribute to protein folding, assembly, and activity. They are involved in various cellular processes, including protein trafficking, transcription, signal transduction, and immune response, making them an essential class of enzymes in all organisms.

    PPIases are widely distributed across species and are categorized into three major families: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. Each family has distinct structural features and evolutionary characteristics. Cyclophilins are primarily found in eukaryotes, while FKBPs are present in both prokaryotes and eukaryotes. Parvulins, on the other hand, are smaller in size and are considered a separate family due to their unique catalytic properties.

    Understanding the function and regulation of peptidylprolyl isomerases is crucial for deciphering the intricate mechanisms underlying protein folding and dynamics. These enzymes serve as important molecular tools for structural biology studies, as their inhibition or manipulation can modulate protein behavior, potentially leading to the development of therapeutic

Common Misspellings for PEPTIDYLPROLYL ISOMERASE

  • oeptidylprolyl isomerase
  • leptidylprolyl isomerase
  • -eptidylprolyl isomerase
  • 0eptidylprolyl isomerase
  • pwptidylprolyl isomerase
  • psptidylprolyl isomerase
  • pdptidylprolyl isomerase
  • prptidylprolyl isomerase
  • p4ptidylprolyl isomerase
  • p3ptidylprolyl isomerase
  • peotidylprolyl isomerase
  • peltidylprolyl isomerase
  • pe-tidylprolyl isomerase
  • pe0tidylprolyl isomerase
  • pepridylprolyl isomerase
  • pepfidylprolyl isomerase
  • pepgidylprolyl isomerase
  • pepyidylprolyl isomerase
  • pep6idylprolyl isomerase
  • pep5idylprolyl isomerase

Etymology of PEPTIDYLPROLYL ISOMERASE

The word "peptidylprolyl isomerase" is derived from the combination of several terms.

1. "Peptidyl" refers to a peptide, which is a compound made up of amino acids, the building blocks of proteins.

2. "Prolyl" specifically refers to the amino acid proline, which is one of the 20 common amino acids found in proteins.

3. "Isomerase" refers to an enzyme that catalyzes the conversion of one isomer into another.

Therefore, "peptidylprolyl isomerase" specifically denotes an enzyme that catalyzes the isomerization of the peptidyl bond involving proline within a peptide or protein.