Tag: carbohydrate metabolism

A modulator is a type of molecule which either stimulates or inhibits enzyme activity. Those which stimulate enzyme activity are known as inducers while those which inhibit enzyme activity are known as inhibitors. The inhibitors can be competitive, non-competitive or allosteric inhibitors. 

Allosteric means in a different steric conformation or occurrence of more than one shapes. Allosteric modulators bind to a site different from the active site and bring changes in the shape or conformation of the enzyme molecule. The change in shape can activate the enzyme or inhibit the activity of enzyme. An allosteric inhibitor will bind to allosteric site and bring in the conformational changes to reduce the enzyme activity.

Competitive inhibition is the inhibition of an enzyme by an inhibitor which has structural similarity to the active site and thus competes with the substrate for binding with the active site. Competitive inhibition is a reversible inhibition and depends on the relative concentration of substrate and inhibitor.

Feedback inhibition is the inhibition mechanism in metabolic pathways where the end product of one reaction are the substrates for next reaction. Such feedback inhibition is usually directed at the first or first few reactions in the pathway to help conserve precious cellular resources, thus in case the end product is not required the metabolic pathway is blocked at the initial stages itself. The feed back regulation is mostly brought about by the allosteric modulators. Usually the first steps in metabolic pathways are catalysed by allosteric enzymes whose catalysis rate can be increased with the help of positive modulators and decreased with the help of negative modulators.

A non-competitive inhibitor is one that binds to a site distinct from the site which binds the substrate; inhibitor binding does not block substrate binding or vice versa. The enzyme is inactivated when inhibitor is bound, whether or not substrate is also present. The inhibitor effectively lowers the concentration of active enzyme and hence, lowers the apparent V$ _{max}$. There is often little or no effect on K$ _m$.

A competitive inhibitor is a reversible inhibition where the inhibitor competes with the substrate for the active site of an enzyme. While the inhibitor occupies the active site it prevents binding of the substrate to the enzyme. Many competitive inhibitors are compounds that resemble the substrate and combine with the enzyme to form an enzyme inhibitor complex, but without leading to catalysis. Even fleeting combinations of this type will reduce the efficiency of the enzyme. By taking into account the molecular geometry of inhibitors that resemble the substrate, we can reach conclusions about which parts of the normal substrate bind to the enzyme. Competitive inhibition can be analyzed quantitatively by steady-state kinetics.

Competitive inhibitors of enzymes compete with the active site of enzyme making them unavailable for the originally desired substrate. 

Succinate was placed in one of the most important cyclic pathways in metabolism, a collecting pool of catabolic and a starting point of many anabolic processes. Succinate is a product of substrate-level phosphorylation materialized in the citric acid cycle. It is involved in a macrophage-specific metabolic pathway generating and is also a downstream product of the α-ketoglutarate dehydrogenase complex, a heavily regulated multi-subunit complex.