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The cells are in a dynamic state where biochemical reactions are highly regulated,
therefore the enzymes that enhance such reactions need to be regulated as well. Enzymes
are regulated in the cells by compartmentation, covalent modification, allosteric regulation,
proteolytic activation and transcriptional control.

(1) Comparmentation enzymes are usually localized within a region or organelle in the
cells. For example, the acid hydrolases that degrade worn out organelles and
biomolecules, are confined within the lysosomes. If these enzymes are released to the
cytoplasm, they will degrade other cell organelles. In addition, the acidic pH in the
lysosome optimizes the activity of these enzymes. Meanwhile, the enzymes involved in
the energy metabolism of the cell, is localized in the mitochondria where they are further
distributed in the inter-membrane space, inner membrane, or the matrix.

(2) Covalent Modification the reversible attachment of a chemical group to specific

amino acid residues in the enzyme may result to its activation or deactivation. The
attachment of phosphate group (phosphorylation) is the most common way of regulating
the activity of an enzyme. This is accomplished either by cyclic adenosine
monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), or kinase
enzymes. Phosphate is attached on serine, threonine, or tyrosine residues of the
enzyme. Phosphate adds a large negative charge to the enzyme that changes its
conformation. This leads to an increase or a decrease in the activity of the enzyme.

(3) Allosteric Regulation this is the noncovalent binding of small molecules called
effectors to sites in the enzyme other than the active site. The interaction induces
conformational changes that activate or deactivate the enzyme. The enzymes that are
acted upon by such effectors are known as allosteric enzymes. They are made up of
several subunits that contain various regulatory sites. Feedback inhibition is the
deactivation of an allosteric enzyme by one of its end products. This is the usual way of
regulating a multi-step reaction pathway.

(4) Proteolytic Modification this is the removal of some amino acid residues from an
inactive enzyme to convert it to its active form. Some enzymes and proteins are
synthesized in inactive forms called zymogens. This is especially true for the digestive
enzymes. For example both trypsin and chymotrypsin are synthesized as the inactive
trypsinogen and chymotrypsinogen respectively. Specific amino acid residues are
removed and the fragments are joined by disulfide bridges to make the enzymes functional.

(5) Transcriptional Control - this is the regulation of the genes that encode for a particular
enzyme. Regulatory substances like hormones and growth factors, can directly or
indirectly affect the expression of these genes. If the regulatory substance is polar, it binds
to specific receptors in the cell membrane. This turn on a cascade pathway that activates
a series of enzymes and proteins that ultimately affects gene expression. If the regulatory
substance is non-polar, it crosses the cell-membrane and bind to specific cytoplasmic
receptors. The complex formed passes through the nucleoplasm and binds directly to a
specific segment in the DNA to affect gene expression of certain enzymes or proteins.