the substrate for lyase is sucrase
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Ligase is an enzyme that catalyzes the joining of two molecules by forming a new chemical bond, usually between nucleic acid strands. Lyase is an enzyme that catalyzes the cleavage of a molecule into two separate molecules without the addition of water. In summary, ligase joins molecules, while lyase splits molecules.
Lyase enzymes are found throughout the human body, with different specific lyase enzymes located in various organs and tissues. They play critical roles in various metabolic pathways by catalyzing the removal or addition of functional groups to substrates. Examples include carbon-carbon lyases found in the liver and kidney that are involved in amino acid metabolism.
Phosphoenolpyruvate carboxykinase (PEPCK) is an enzyme in the lyase family.
Lyase enzymes catalyze the breaking of chemical bonds in molecules without using water, while ligase enzymes catalyze the formation of new bonds between molecules using energy from ATP. Lyase enzymes work by eliminating groups from substrates, while ligase enzymes work by joining two molecules together.
enzyme-substrate complex
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in an enzyme-substrate complex, the enzyme acts on the substrate .
Substrate.
The substrate of protease is a peptide bond.
When an enzyme and substrate come together, it is called the enzyme-substrate complex. This complex is a temporary intermediate state in which the enzyme binds to the substrate to catalyze a chemical reaction.
A substrate is the substance in which an enzyme act, or a process occurs. For example lactose is a substrate, but water is not.