Template/lock and key theory of enzyme action is supported by the fact that
Template/lock and key theory of enzyme action is supported by the fact that
The correct option is C Compounds similar to substrate inhibit enzyme activity
Every enzyme has an active site,
by means of which its cognate substrate binds to it. When the amino acids fold
into their higher order structure, they form a 3-D structure, with clefts
having a complementary conformation of its preferred substrate. Thus, the
substrate binds to the enzyme and fits like a key in a lock. The active site
cleft not only provides a physical scaffold for substrate binding but also has
amino acids which are crucial for the enzymatic activity. When the substrate
binds to its enzyme at the active site, those amino acids carry on the chemical
reaction and bring about the change of substrate, yielding product. Generally, the
product, having a different conformation than substrate can no longer bind to
the cognate cleft of active site and is hence released from the enzyme. Inhibitors
of the enzyme usually mimics the substrate conformation and can easily bind to
the enzyme active site (due to conformational compatibility) but cannot be
acted upon by the active site amino acids, hence enzyme would be rendered inactive.
Hence this supports the lock and key theory of enzyme substrate interaction. So, the correct answer is 'Compounds similar to substrate inhibit enzyme activity'.
Every enzyme has an active site,
by means of which its cognate substrate binds to it. When the amino acids fold
into their higher order structure, they form a 3-D structure, with clefts
having a complementary conformation of its preferred substrate. Thus, the
substrate binds to the enzyme and fits like a key in a lock. The active site
cleft not only provides a physical scaffold for substrate binding but also has
amino acids which are crucial for the enzymatic activity. When the substrate
binds to its enzyme at the active site, those amino acids carry on the chemical
reaction and bring about the change of substrate, yielding product. Generally, the
product, having a different conformation than substrate can no longer bind to
the cognate cleft of active site and is hence released from the enzyme. Inhibitors
of the enzyme usually mimics the substrate conformation and can easily bind to
the enzyme active site (due to conformational compatibility) but cannot be
acted upon by the active site amino acids, hence enzyme would be rendered inactive.
Hence this supports the lock and key theory of enzyme substrate interaction. So, the correct answer is 'Compounds similar to substrate inhibit enzyme activity'.
