How Do You Spell ARGININE CARBOXYPEPTIDASE?

Pronunciation: [ˈɑːd͡ʒɪnˌa͡ɪn kˈɑːbəksˌa͡ɪpptɪdˌe͡ɪs] (IPA)

Arginine carboxypeptidase is a protein-digesting enzyme responsible for cleaving peptide bonds at the carboxyl end of arginine residues. Its spelling can be challenging for those unfamiliar with the specialized terminology used in biochemistry. The IPA phonetic transcription of the word "arginine carboxypeptidase" is /ˈɑːrɡɪniːn kɑːrˌbɒksipɛptaɪdeɪs/, with stress on the first syllable of both "arginine" and "carboxypeptidase". This phonetic transcription helps to clarify the pronunciation of this complex term for those who may find it difficult to read or say at first glance.

ARGININE CARBOXYPEPTIDASE Meaning and Definition

1. Arginine Carboxypeptidase is a type of enzyme that belongs to the carboxypeptidase family. It is primarily involved in the hydrolysis of peptide bonds in proteins or peptides, specifically at the carboxyl terminal end of arginine residues. This enzymatic activity is essential for the degradation of proteins, the formation of bioactive peptides, and the regulation of various physiological processes.

   Arginine Carboxypeptidase is commonly found in bacteria, fungi, and some animals, including humans. It is synthesized as an inactive precursor or zymogen, which is then activated by proteolytic cleavage in specific conditions. The active form of the enzyme consists of a single polypeptide chain and requires divalent metal ions, such as zinc, for its optimal activity.

   The catalytic mechanism of Arginine Carboxypeptidase involves the nucleophilic attack of a water molecule on the carboxyl carbon of the peptide bond, resulting in the release of the carboxyl group of the amino acid residue. The enzyme typically exhibits high specificity for arginine residues, although some variations of this enzyme may also exhibit activity towards other amino acids.

   The biological functions of Arginine Carboxypeptidase are diverse and depend on the specific organism and tissue in which it is present. It plays a crucial role in protein turnover, peptide hormone processing, cell signaling, and the regulation of blood pressure. Abnormalities in Arginine Carboxypeptidase activity or expression have been associated with various diseases, including hypertension, metabolic disorders, and certain types of cancer. Research on this enzyme is ongoing to better understand its physiological and pathological significance.

Common Misspellings for ARGININE CARBOXYPEPTIDASE

• zrginine carboxypeptidase
• srginine carboxypeptidase
• wrginine carboxypeptidase
• qrginine carboxypeptidase
• aeginine carboxypeptidase
• adginine carboxypeptidase
• afginine carboxypeptidase
• atginine carboxypeptidase
• a5ginine carboxypeptidase
• a4ginine carboxypeptidase
• arfinine carboxypeptidase
• arvinine carboxypeptidase
• arbinine carboxypeptidase
• arhinine carboxypeptidase
• aryinine carboxypeptidase
• artinine carboxypeptidase
• argunine carboxypeptidase
• argjnine carboxypeptidase
• argknine carboxypeptidase
• argonine carboxypeptidase

Etymology of ARGININE CARBOXYPEPTIDASE

The word "Arginine Carboxypeptidase" has a specific etymology derived from its components.

1. Arginine: The term "arginine" originates from the Greek word "árgos", meaning "idle", and the ending "-ine", which is used in chemistry to denote a compound. It was initially isolated from the extract of lupin seedlings in 1886, and it refers to an essential amino acid that plays a crucial role in various biological processes.

2. Carboxypeptidase: The term "carboxypeptidase" is composed of two elements. "Carboxy" comes from "carboxyl", which refers to the carbon atom attached to an oxygen atom through a double bond and a hydroxyl group. "Peptidase" derives from "peptide", which describes short chains of amino acids linked by peptide bonds.