The R groups of the amino acids in its active site
The order in which aminoacids are encoded.
Pie
tertiary
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
Yes.
Quaternary and Tertiary levels of protein structure principally determine the active site of an enzyme.
ATP synthase
Catalysts are compounds that change the speed of chemical reactions. An enzyme is a protein and also a catalyst. So an enzyme can be a catalyst, but a catalyst can't be an enzyme.
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
The enzyme's surface folds are complementary to the substrate's surface folds.
What an enzyme does is based on its shape, therefore you would have to change it on a molecular level in order to alter its job.
Yes.
Quaternary and Tertiary levels of protein structure principally determine the active site of an enzyme.
ATP synthase
Catalysts are compounds that change the speed of chemical reactions. An enzyme is a protein and also a catalyst. So an enzyme can be a catalyst, but a catalyst can't be an enzyme.
1) absolute specificity 2) Group specificity 3) Linkage specificity 4) Stereochemical specificity
The allosteric site is distinct from the active site, and does not affect the substrate specificity of the enzyme
Actually it is. It is a polypeptide structure that has been specialized to be a catalyst.
Yes, enzymes are proteins and it is their sequence of amino acids (primary structure) that determines what kind of an enzyme it is and makes all the enzymes unique and it is the tertiary structure of enzymes that maintains their shape and give rise to the unique active site. When an enzyme is denatured, it loses its tertiary structure and therefore its shape.
The alteration of an amino acid on a site other than the active site will: change the shape of the protein.