Trypsin, lipase, chymotrypsin, pancreatic amylase, steapsin, elastases, carboxypeptidase, and nucleases. ~answered by FightingLucario
The digestive enzymes produced by the pancreas are typically produced as inactive precursors (zymogens). These inactive forms are activated in the digestive tract when specific proteases cleave them to their active forms, ensuring they are only active when needed for digestion.
Trypsin, lipase, chymotrypsin, pancreatic amylase, steapsin, elastases, carboxypeptidase, and nucleases. ~answered by FightingLucario
Trypsin, lipase, chymotrypsin, pancreatic amylase, steapsin, elastases, carboxypeptidase, and nucleases. ~answered by FightingLucario
Proteolytic enzymes will destroy the cells that produced them if they are produced in an active form. To protect the body's own cells these enzymes are secreted in an inactive form into the digestive tract and activated where they are needed.
We need more information as to which enzymes you are asking about.
There are many different types of enzymes because each type have a differently shaped active site (the place where the reaction takes place) and the reaction can only happen if the active site is the right shape for the food molecule. eg. Protease enzymes break down proteins.
The substrate for enterokinase is trypsinogen, an inactive precursor of the digestive enzyme trypsin. Enterokinase, produced in the intestine, activates trypsinogen by cleaving it to form active trypsin. This activation is crucial for the digestive process, as trypsin further activates other proteolytic enzymes.
Trypsin, lipase, chymotrypsin, pancreatic amylase, steapsin, elastases, carboxypeptidase, and nucleases. ~answered by FightingLucario
Trypsin, lipase, chymotrypsin, pancreatic amylase, steapsin, elastases, carboxypeptidase, and nucleases. ~answered by FightingLucario
No, uncompetitive inhibitors do not bind to the active site of enzymes. They bind to a different site on the enzyme, causing a conformational change that prevents the substrate from binding to the active site.
Enzyme specificity is mainly determined by the unique structure of their active site, which allows them to bind to specific substrates. This specificity arises from the unique sequence and conformation of amino acids that make up the active site, which are dictated by the enzyme's genetic code. Additionally, the 3D shape of enzymes is influenced by their environment, such as temperature and pH, which can affect their function and specificity.
Pepsin is the primary digestive enzyme that is active under strongly acidic conditions, specifically in the stomach where the pH can be as low as 1.5 to 3.5. It is responsible for breaking down proteins into smaller peptides. Additionally, gastric lipase also functions in the acidic environment of the stomach, aiding in the digestion of fats. These enzymes are adapted to operate effectively in the low pH of gastric juice.