BIOC 1430 Lecture Notes - Lecture 14: Non-Competitive Inhibition, Histidine Decarboxylase, Competitive Inhibition

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2 Apr 2016

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Inhibition is loss of catalytic activity of enzymes. Enzyme inhibitors are substances that slow or stop the normal catalytic function of an enzymes by biding to it. A change in protein structure occurs so that the active site is prevented from binding with its proper substrate. There are 3 modes by which this inhibition can take place: reversible competitive inhibition, reversible non-competitive inhibition. Occurs when a compound with a structure very similar to the substrate competes for the active site on the enzyme this competitive inhibitor fits in to the active site of the enzyme. As long as the inhibitor occupies the active site, the substrate cannot bind to it, resulting in decreased enzyme activity. Held together by weak interaction; will break up over time. Empty active site is ready for new occupant. On a random basis, either inhibitor or normal substrate will bind. By increasing the substrate concentration competitive inhibition is reversed.

Related Questions

A variety of factors influence enzyme activity. Substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. Identify the type of inhibition associated with each of the following descriptions and examples by sorting each item into the appropriate bin.

The bins are: irriversible inhibition, compenitive inhibition, mixed inhibition

The phrases to sort are:

-Tamiflu, a transition state analog, reversibly binds to neuraminidase

- Inhibitor may perminantely modify an enzyme

-DIPF permanently modifies the hydroxyl group of a Ser residue at the active site

- the AL3+ ion binds to acetylcholinesterase or to the acetylcholinesterase-substrate complex

- binding by the inhibitor does not affect VMax

-Binding by the inhibitor decreases VMax

Can you please answer my questions fast I appreciate it no explanation is needed

B. C. Mixed tive 8. The panereas is protected from digestion by trypsin (a proteolytic enzyme that it produces) because: A. B. C. D. Trypsin works only on denatured proteins Trypsin is specific for plant proteins Trypsin works only at the surface of membranes Trypsin is not activated until it is proteolytically modified 9. The active site of an enzyme is the region that A. binds allosteric regulators of the enzyme. B. is involved in the catalytic reaction of the enzyme C. binds noncompetitive inhibitors of the enzyme D. is inhibited by the presence of a coenzyme or a cofactor 10. According to the induced fit hypochesis of enzyme catalysis,which of the following is corect? A. The binding of the substrate depends on the shape of the active site B. Some enzymes change their structure when activators bind to the enzyme C. A competitive inhibitor can outcompete the substrate for the active site D. The binding of the substrate changes the shape of the enzyme's active site 11. Increasing the substrate concentration in an enzymatic reaction could overcome which of the following? A. denaturization of the enzyme B. allosteric inhibition C competitive inhibition D. saturation of the enzyme activity 12. Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as a(n) A. competitive inhibitor of the enzyme B. noncompetitive inhibitor of the enzyme C. allosteric activator of the enzyme. D cofactor necessary for enzyme activity 13. Some of the drugs used to treat HIV patients are competitive inhibitors of the HIV reverse transcriptase enzyme. Unfortunately, the high mutation rate of HIV means that the virus rapidly acquires mutations with amino acid changes that make them resistant to these competitive inhibitors. Where in the reverse transcriptase enzyme would such amino acid changes most likely occur in drug-resistant viruses? A. in or near the active site B. at an allosteric site Cat a cofactor binding site D. in regions of the protein that determine packaging into the virus capsid the fever is not controlled? When you have a severe fever, what grave consequence may occur if A. destruction of your enzymes' primary structure B. removal of amine groups from your proteins C. change in the tertiary structure of your enzymes D removal of the amino acids in active sites of your enzymes 14.

BIOC 1430 Lecture Notes - Lecture 14: Non-Competitive Inhibition, Histidine Decarboxylase, Competitive Inhibition

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