It will most likely be naturalized (rendered a useless carbon chain) as the acidic H3O- Hydronium particles in the acid will donate the extra Hydrongen particle and saturate the enzyme causing it to lose it's shape and/or reactivity and therefore lose its effetiveness .
Alex PH
Aminoacyl-tRNA synthetase is the enzyme responsible for catalyzing the attachment of an amino acid to tRNA. This process is vital for protein synthesis, ensuring that the correct amino acid is paired with its corresponding tRNA molecule.
The citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle) involves co-enzyme A, NAD+, and FAD. This metabolic pathway takes place in the mitochondria and is a central process in the generation of ATP from carbohydrates, fats, and proteins.
NADH levels would increase in the cell due to the build-up of acetyl CoA, as it cannot be converted to citrate. This is because the enzyme responsible for converting acetyl CoA to citrate is inhibited, leading to a block in the tricarboxylic acid (TCA) cycle and subsequent accumulation of NADH.
There are many possibilities. If the mutations occurs but it does not change the amino acid sequence due to the redundancy (codon degeneracy) of the genetic code, then the mutation is silent and no effect is observed. If the mutation occurs and the amino acid sequence is changed, but the new amino acid has similar properties to the original amino acid (e.g. aspartic acid -> glutamic acid) and the position of the mutation is far away from the active site, then the mutation will likely have minimal effects on the structure and function of the protein. However, if the mutation changes the amino acid sequence such that the new amino acid has a very different property to the original (lysine -> valine) or if the mutation occured close to the acitive site, then it is very likely that the structure and function of the protein will be compromised. Lastly, there is also the marginal chance that the last type of mutation described above actually increases the effectiveness of the protein. Though this is exceedingly rare, it is the driving force behind evolution.
The active site of an enzyme is where the substrate binds and where the chemical reaction catalyzed by the enzyme takes place. The active site provides specific amino acid residues that interact with the substrate to facilitate the reaction, leading to the formation of the product. The enzyme-substrate complex is formed at the active site, which stabilizes the transition state and lowers the activation energy of the reaction.
acid
The reactant for the enzyme aspartase is aspartic acid. It catalyzes the conversion of aspartic acid into fumaric acid.
That chemical would be hydrochloric acid.
it would contridict the acid and nothing would happen ! Anacid neutralises acid & salts get formed !
it alters the pH of the enzyme denaturing it leaving it unable to carry out it's role effectively or at all
pepsin
Pepsin
Enzymes break down proteins, not acids.
Acid hydrolysis of sucrose involves using acids to break down the sugar molecule, while enzyme invertase specifically catalyzes the breakdown of sucrose into glucose and fructose. Employing acid hydrolysis would interfere with the enzyme's function by disrupting its structure or activity, ultimately thwarting the experiment’s objective of studying invertase's enzymatic action on sucrose.
acetyl CoA or Acetyl Co-enzyme A is required for fatty acid synthesis
Aminoacyl-tRNA synthetase is the enzyme responsible for catalyzing the attachment of an amino acid to tRNA. This process is vital for protein synthesis, ensuring that the correct amino acid is paired with its corresponding tRNA molecule.
Acid in orange juice is important for the color, flavor, and nutritional quality. Without acid, the color will likely be different due to enzyme action and pH effects on pigments. It will probably be a brownish color. The sour flavor would also be missing. Lastly, certain vitamins and minerals would be more easily destroyed or indigestible.