Aspartokinase is a 14-letter word used in biochemistry. It is pronounced as /əˌspɑːtəʊˈkaɪneɪs/ according to IPA phonetic transcription. The first syllable starts with the unstressed schwa sound, followed by the stressed /ɑː/ sound. The second syllable starts with /t/ followed by an unstressed /əʊ/ and stressed /kaɪ/ sounds. The final syllable starts with the unstressed schwa sound, followed by the stressed /neɪs/ sound. The word refers to an enzyme that converts aspartic acid to aspartate semialdehyde in a metabolic pathway.
Aspartokinase is an enzyme that plays a crucial role in the metabolic pathway known as the aspartate family amino acid biosynthesis pathway. It catalyzes the conversion of L-aspartate and ATP (adenosine triphosphate) into beta-aspartyl phosphate and AMP (adenosine monophosphate). This enzyme is mainly found in bacteria and some plants, where it is an essential component in the production of certain amino acids.
Aspartokinase is classified as a transferase enzyme, specifically a phosphoryl transferase, as it transfers the phosphate group from ATP to L-aspartate during the reaction. The enzyme acts as a key regulator in the biosynthesis of the amino acids lysine, threonine, and methionine. It controls the rate of the pathway by responding to the concentration of these amino acids, ensuring a balanced production to meet the cellular needs.
The structure of aspartokinase consists of multiple subunits that come together to form an active enzyme. Each subunit has a unique role in carrying out the catalytic reaction, ensuring the efficiency of the conversion process. Aspartokinase is subject to regulation through feedback inhibition, where the end products of the aspartate family amino acid biosynthesis pathway can bind to the enzyme and inhibit its activity, preventing excessive production of these amino acids.
Overall, aspartokinase is a vital enzyme in the biosynthesis of specific amino acids and is essential for maintaining the balance of aspartate family amino acids within cells.
The word "aspartokinase" is derived from three different components: "asparto-", "kine-", and "-ase".
The prefix "asparto-" refers to aspartic acid, an amino acid found in proteins. It is derived from the Latin term "asparaginum", which refers to an amino acid present in asparagus.
The term "kine-" is derived from the Greek word "kinēsis", which means motion or movement. In the context of enzymes, it refers to the catalytic activity these proteins exert.
Finally, the suffix "-ase" is commonly used in biochemistry to denote enzymes. It is derived from the Greek word "asis", meaning "action" or "process".
Combining these components, "aspartokinase" refers to an enzyme that catalyzes the phosphorylation of aspartic acid, specifically converting it into β-aspartyl phosphate.