how do enzymes differ from inorganic catalists ?

Enzymes Inorganic catalysts
They are mostly globular proteins, some are ribonucleotides (ribozymes). They are inorganic molecules or ions.
 
They are very specific about the substrate.   One catalyst can work upon diverse substrates.
Their activity is regulated very precisely by regulator molecules. No such regulator mechanism exists.
 
They are very sensitive to temperature and pH and work best  in an optimum range and denature above or below it. They are less sensitive to temperature and pH.
They are synthesised in an organism's body as coded by its genome.  They are not synthesised in the living cells and can be found in soil etc.
Examples include carboxylases, polymerases etc. Examples include zinc, magnesium etc.

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please reply this answer i am waiting 
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As you know, a catalyst is a substance that alters the rate of a reaction by decreasing the activation barrier. Inorganic catalysts are usually composed of metals( for instance Fe in Haber Process and V in Ostwald process) which mainly employs the idea of providing more surface area and thereby decreasing the activation of energy for a reaction. Organic catalysts in the other hand is composed mostly of organic molecules like amino acids (Enzymes) and Nucleic acids (eg: Ribosome. In ribosomes where amino acids join together to form proteins, the active site, where the reaction take place is composed of RNA molecules). The major difference between inorganic catalysts and organic catalysts are organic catalysts are stereospecific, that is, enzymes that could catalyze a reaction might not be able to catalyze a reaction with a different substrate (eg : Hexokinase, an enzyme that adds phosphate group to C6 carbon of glucose can't add a phosphate group to fructose, which is an isomer of glucose) ​ while most inorganic catalysts are not stereo specific.

Hope this helps.
 
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