Since Eduard Büchner won the Nobel Prize in Chemistry in 1907, the world has once again valued enzymes. Scientific research activities have become more frequent and in-depth. The natural properties of enzyme proteins have also been revealed. Several famous theories have been put forward as enzymes—the basis of theoretical research on catalysis.
Beginning around 1894, German organic chemist Emil Fisher began to study the primary content of enzyme catalysis and proposed the famous “lock and key theory” of the interaction between enzymes and substrates. British chemist Adrian Brown (Adrian Brown) and French biochemist Victor Henri (Victor Henri) proposed the intermediate product theory of enzymes in 1902 and 1903, respectively. In 1913, German biochemists Leonor Michaelis (Leonor Michaelis) and Maud Menten ((Maud Menten) proposed the “rapid equilibrium theory” based on the theory of intermediate products. They deduced the fundamental dynamics of enzymatic reaction kinetics. This is an essential breakthrough in the study of enzyme reaction mechanisms.
In the early 20th century, the properties of enzymes were still unknown, and many scientists observed the correlation between enzyme activity and proteins, but the most direct evidence was still lacking. In 1926, American biochemist James B. Sumner (James B. Sumner) obtained the crystallization of urease from sword bean seeds for the first time and confirmed for the first time that urease is a protein through chemical experiments. American biochemists Northrop (Northrop) and Kunitz (Kunitz) obtained more enzyme crystals (such as pepsin, trypsin, and chymotrypsin) in 1930-1936. They confirmed it chemically Enzyme is a kind of protein, and then the essence of the enzyme is people generally accept protein. Sumner and Northrop shared the Nobel Prize in Chemistry in 1949. Now that we know that enzymes have catalytic properties, what is the law of catalysis? People need to be faster to recognize. In 1958, American chemist Daniel E. Koshland (Daniel E. Koshland) realized that the structure of enzymes is flexible in catalysis. Based on this, he proposed the “induced fit theory.” Later, the French biochemist Monod proposed an “allosteric model” in 1961 to explain quantitatively that small binding molecules can regulate the activity of enzymes. In 1982, American biologist Cech and chemist Altman discovered RNA with catalytic function—ribozyme. Cech found that an RNA precursor in Tetrahymena cells has the role of self-splicing. Altman discovered that the RNA part of ribonuclease has catalytic activity, breaking the traditional concept that enzymes are proteins. Altman was jointly awarded the Nobel Prize in Chemistry in 1989. This is also the last Nobel Prize in the field of enzymes.