Tag: enzyme properties

Enzymes are inducible in nature because as the substrate molecules attaches to the active site of the enzyme, it induces a conformational change on the active site to fit in properly.

Hydrolytic reactions are the reactions which involves breaking of the bond by the addition of water. It can be reversed by the condensation reaction where the joining of two molecule leads to release of water by formation of bonds. Saccharification is the reaction where the complex sugar molecule is broken into its component sugar molecules by hydrolysis. It can be reversed by condensation reaction.

The optimum temp of enzymes is 20-35°C. They become inactivated at very low temperature and denatured (destroyed) at very high temp i.e. greater than 45°C. Low molecular weight enzymes are comparatively more heat stable. In archaebacterium Pyrococcus furiosus, the optimum temperature of hydrogenase is greater than 95°C. This heat-stable enzyme enables Pyrococcus to grow at 100°C. The optimum pH of most endoenzyme is pH 7.0 (neutral pH). However, digestive enzymes can function at different pH. For example, salivary amylase act best at pH 6.8, pepsin act best at pH2 etc. Any fluctuation in pH from the optimum causes ionization of R-groups of amino acids which decrease the enzyme activity.

Serine proteases are enzymes that cleave peptide bonds in proteins, in which serine serves as a nucleophilic amino acid at enzyme's active site. Serine proteases are responsible for coordinating various physiological functions including digestion, immune response, blood coagulation, and reproduction. Hence, serine proteases are called so because they require serine for their activity.

FAD also is known as Flavin Adenine Dinucleotide. It is a redox-active co-enzyme associated with various proteins. Riboflavin is the precursor of FAD.

The enzyme active site is composed of the amino acid residues. Side chains of the amino acids are seen in the active site region of the enzyme. The difference in the identity, charge, and spatial orientation of the functional groups located there results in the difference in enzyme specificity.