Study the following

I)  $K_m$ value               Affinity of the enzyme      Inverse measure enzyme affinity

II) Hydrolases             P-O bonds                          Linking 2 compounds

III) Transferases          Transfer of a group            Inhibitor of reaction

IV) Emil Fisher           Lock and key hypothesis   Formation of ES complex

Identify the incorrect combinations.

Km is a measure of enzyme affinity. It is the substrate concentration at which the reaction rate is half of the maximum rate and is an inverse measure of enzyme affinity - a lower Km value indicates higher affinity of the enzyme for its substrate.

Emil Fisher proposed the lock and key hypothesis, which suggests that the binding between an enzyme and its substrate is highly specific, like a key fitting into a lock. This binding results in the formation of an enzyme-substrate complex (ES complex), which then undergoes a chemical reaction to form the product.

Enzymes catalysing hydrolysis of ester, ether, peptide, glycosidic, C-C, C-halide or P-N bonds. Ligases  catalysing the linking together of 2 compounds, e.g., enzymes which catalyse joining of C-O, C-S, C-N, P-O etc. bonds.

Transferases are enzymes catalysing a transfer of a group, G (other than hydrogen) between a pair of substrate S and S’.