What makes proteins the ideal types of compounds to act as enzymes?


An energy-releasing reaction is more likely to start spontaneously. You have to have enough energy to overcome the activation energy barrier (that is to start breaking some bonds). Viva la AnswerParty!

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proteins Chemistry
Physical chemistry

Physical chemistry is the study of macroscopic, atomic, subatomic, and particulate phenomena in chemical systems in terms of laws and concepts of physics. It applies the principles, practices and concepts of physics such as motion, energy, force, time, thermodynamics, quantum chemistry, statistical mechanics and dynamics, equilibrium.

Physical chemistry, in contrast to chemical physics, is predominantly (but not always) a macroscopic or supra-molecular science, as the majority of the principles on which physical chemistry was founded, are concepts related to the bulk rather than on molecular/atomic structure alone. For example, chemical equilibrium, and colloids.

Catalysis Metabolism
Chemical kinetics

Chemical kinetics, also known as reaction kinetics, is the study of rates of chemical processes. Chemical kinetics includes investigations of how different experimental conditions can influence the speed of a chemical reaction and yield information about the reaction's mechanism and transition states, as well as the construction of mathematical models that can describe the characteristics of a chemical reaction. In 1864, Peter Waage and Cato Guldberg pioneered the development of chemical kinetics by formulating the law of mass action, which states that the speed of a chemical reaction is proportional to the quantity of the reacting substances.

Chemical kinetics deals with the experimental determination of reaction rates from which rate laws and rate constants are derived. Relatively simple rate laws exist for zero-order reactions (for which reaction rates are independent of concentration), first-order reactions, and second-order reactions, and can be derived for others. In consecutive reactions, the rate-determining step often determines the kinetics. In consecutive first-order reactions, a steady state approximation can simplify the rate law. The activation energy for a reaction is experimentally determined through the Arrhenius equation and the Eyring equation. The main factors that influence the reaction rate include: the physical state of the reactants, the concentrations of the reactants, the temperature at which the reaction occurs, and whether or not any catalysts are present in the reaction.

Energy Enzyme
Activation energy

In chemistry, activation energy is a term introduced in 1889 by the Swedish scientist Svante Arrhenius that is defined as the minimum energy that must be input to a chemical system, containing potential reactants, in order for a chemical reaction to occur. Activation energy may also be defined as the minimum energy required to start a chemical reaction. The activation energy of a reaction is usually denoted by Ea and given in units of kilojoules per mole.

Activation energy can be thought of as the height of the potential barrier (sometimes called the energy barrier) separating two minima of potential energy (of the reactants and products of a reaction). For a chemical reaction to proceed at a reasonable rate, there should exist an appreciable number of molecules with energy equal to or greater than the activation energy.

Enzyme catalysis

Enzyme catalysis is the catalysis of chemical reactions by specialized proteins known as enzymes. Catalysis of biochemical reactions in the cell is vital due to the very low reaction rates of the uncatalysed reactions.]citation needed[

The mechanism of enzyme catalysis is similar in principle to other types of chemical catalysis. By providing an alternative reaction route the enzyme reduces the energy required to reach the highest energy transition state of the reaction. The reduction of activation energy (Ea) increases the amount of reactant molecules that achieve a sufficient level of energy, such that they reach the activation energy and form the product.

Peptide bond

A peptide bond (amide bond) is a covalent chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, causing the release of a molecule of water (H2O), hence the process is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids. The resulting C(O)NH bond is called a peptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called a peptide link. Polypeptides and proteins are chains of amino acids held together by peptide bonds, as is the backbone of DNA.

A peptide bond can be broken by hydrolysis (the adding of water). In the presence of water they will break down and release 8–16 kilojoule/mol (2–4 kcal/mol) of free energy. This process is extremely slow (up to 1000 years). In living organisms, the process is facilitated by enzymes. Living organisms also employ enzymes to form peptide bonds; this process requires free energy. The wavelength of absorbance for a peptide bond is 190–230 nm (which makes it particularly susceptible to UV radiation).

Environment energy-releasing reaction activation energy barrier

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