Characteristics and mechanism of enzyme action

Biology · Enzymes. The idea in plain words, the rules to remember, the mistake to avoid and a worked example, written and checked by Mega Lecture.

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The idea

Enzymes are biological catalysts. Almost all are globular proteins. They speed up reactions in the cell, are needed in very small amounts, and are unchanged at the end, so they can be used again.

The substrate fits into a small pocket on the enzyme called the active site, forming an enzyme-substrate complex. Because of the shape of the active site an enzyme is specific: it works on one substrate or one group of related substrates.

Every reaction needs a starting push of energy called the activation energy. An enzyme lowers this energy, so the reaction goes quickly at body temperature. It does not change the products or the equilibrium of the reaction.

Rules to remember

Common mistake

Students mix up coenzyme and prosthetic group. Both are non-protein, but a coenzyme is loosely attached and a prosthetic group is covalently bonded to the enzyme; an activator is an inorganic ion.

Worked example

An enzyme stops working when Mg2+ ions are removed from its solution, and works again when the ions are added back. What is Mg2+ for this enzyme?

  1. The enzyme needs a non-protein helper, so Mg2+ is a cofactor.
  2. Mg2+ is an inorganic ion, so it is not a coenzyme (coenzymes are organic).
  3. It can be taken away and put back, so it is detachable, not covalently bonded like a prosthetic group.

Answer: An activator (a detachable inorganic cofactor).

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