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What is the active site for peptides?
The active site for peptides is typically found in the binding pocket of an enzyme, where the peptide substrate interacts with specific amino acid residues to facilitate the enzymatic reaction. This interaction involves the formation of temporary bonds between the enzyme and the peptide substrate, allowing for catalysis of peptide bond formation or cleavage. The active site geometry and amino acid composition are crucial for the enzyme's specificity and efficiency in peptide processing.
What is the reactant for the enzyme peptidase?
The reactant for the enzyme peptidase is a peptide molecule. Peptidase enzymes catalyze the breakdown of peptide bonds within peptides or proteins, resulting in the release of amino acids.
Where is the Chief site of sugar breakdown?
when you have diahreea
What organ is the hydrolysis of protein initiated?
Breakdown of proteins begins in the stomach.
How many molecules of water are used up in the COMPLETE breakdown of a polypeptide that is 15 amino acids in length?
In the complete breakdown of a polypeptide, one water molecule is used for each peptide bond formed between amino acids during the process of hydrolysis. For a 15-amino acid polypeptide, there are 14 peptide bonds formed between amino acids, leading to the consumption of 14 molecules of water during the breakdown.
What enzyme digests peptides?
Proteases, also known as peptidases or proteinases, are enzymes that digest peptides by breaking down the peptide bonds between amino acids in the peptide chain. These enzymes are crucial for the breakdown of proteins into amino acids for absorption and utilization by the body.
What is The bond that links two amino acids called?
This is called a peptide bond, or peptide linkage.
What class of enzyme catalyzes addition of splitting peptide bonds in proteins?
Proteases, also known as peptidases or proteolytic enzymes, are the class of enzymes that catalyze the hydrolysis of peptide bonds within proteins. They facilitate the breakdown of proteins into smaller peptides or individual amino acids.
What is the function of zinc in the active site of the enzyme carboxypeptidase?
Zinc serves as a cofactor in the active site of carboxypeptidase by stabilizing the reaction intermediate during peptide cleavage. It acts as a Lewis acid, facilitating the nucleophilic attack on the peptide bond. Zinc also helps orient the substrate in the active site for optimal binding and catalysis.
What is kallikreinkinin?
Kallikreins are biological enzymes of the peptidase (or protease) group. They cleave the peptide bonds in proteins. More specifically, they are "serine" proteases because they cleave the peptide bond at a site in the protein where there is a serine (an amino acid) molecule.
What are the bonds that are the bonds that hold two amino acids together called?
peptide A.S.Apex :)
What chemical is in a bee sting?
According to the link, below, the major chemical in a honey bee sting is "melittin".
