Step-by-step explanation:
Invertase, also known as beta-fructofuranosidase, is an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. It is a glycoside hydrolase enzyme, which means that it breaks down glycosidic bonds between carbohydrates.
The structure of invertase is complex and consists of several domains. The enzyme is typically a homodimer, which means it is made up of two identical subunits. Each subunit consists of a catalytic domain, a linker region, and a non-catalytic domain.
The catalytic domain contains the active site of the enzyme, where the hydrolysis of sucrose takes place. It consists of a beta-sandwich fold with a central cavity that accommodates the substrate. The catalytic residues are located at the bottom of the cavity, where they interact with the sucrose molecule.
The linker region connects the catalytic domain to the non-catalytic domain and is flexible, allowing for movement of the catalytic domain during the enzymatic reaction.
The non-catalytic domain is located at the C-terminus of the enzyme and is involved in substrate binding and specificity. It contains a fructose-binding domain, which helps to stabilize the fructose molecule during the hydrolysis reaction.
Overall, the structure of invertase is highly conserved across different species, with slight variations in the amino acid sequence and domain arrangement.