ENZYMES (Part 3)

TPP (Thiamine Pyrophosphate)

Vitamin B1

Thiamine

Vitamin B1

FAD (Flavin Adenine Dinucleotide)

Vitamin B2

Riboflavin

Vitamin B2

NAD (Nicotinamide Adenine Dinucleotide)

Vitamine B3

Niacin

Vitamin B3

CoA (Coenzyme A)

Vitamin B5

Pantothenic Acid

Vitamin B5

PyP (Pyridoxal Phosphate)

Vitamin B6

Peridoxyne

Vitamin B6

Biocytin

Vitamin B7

Biotin

Vitamin B7

THFA (Tetrahydrofolic Acid)

Vitamin B10

Folic Acid

Vitamin B10

Deoxyadenosyl Cobalamin

Vitamin B12

Cobalamin

Vitamin B12

Coenzymes

Are organic compounds that are endowed with specific structural features that allow them to help accelerate the enzymatic reactions. They function as carriers of atoms or electrons which are essential for normal metabolism.

Pyridoxal Phosphate

Coenzyme ________ aids in the transfer of amino group and phosphate group.

FAD & NAD

Coenzymes _________ aids in all oxidation-reduction reactions.

THFA

Coenzyme ________ is responsible for the acceleration of a number of enzymatic reactions involving activation of one carbon fragment such as in formyl and methylene.

Deoxyadenosyl Cobalamin

Coenzyme __________ aids in the amino acid metabolism and failure of the body to absorb Cobalamin (Vitamin B12) results in pernicious anemia.

Acetaldehyde

Ethyl Alcohol + Zn Alcohol Dehydrogenase+ NAD → ____________ + NADH + Enzyme

• Enzyme: Zn Alcohol Dehydrogenase

• Classification of Enzymes: Oxido-reductase

• Coenzyme: NAD

• Product: ____________

Fumaric Acid

Succinic Acid + Succinic Acid Oxidase + NAD → ____________ + NADH + Enzyme

• Enzyme: Succinic Acid Oxidase

• Classification of Enzymes: Oxido-reductase

• Coenzyme: NAD

• Product: ____________

Lyase

Acetoacetic Acid + Decarboxylase + TPP → Acetaldehyde + Carbon Dioxide + Enzyme

• Enzyme: Decarboxylase

• Classification of Enzymes: _________

• Coenzyme: TPP

• Product: Acetaldehyde

Pyruvic Acid

Alanine + alpha-keto Glutaric Acid + Transaminase + Peridoxal Phosphate → ___________ + Glutamic Acid

• Enzyme: Zn Alcohol Dehydrogenase

• Classification of Enzymes: Transferases

• Coenzyme: PyP

• Product: ____________

Inhibitors

Cofactors and Coenzymes are small non-protein molecules that enhance the enzyme’s function while _________ deactivates enzymes to purposely slow their activity temporarily or permanently.

Inhibition

The binding of enzymes to the active sites, causes the inhibitors to reduce the compatibility of substrate and enzyme and this leads to the inhibition of enzyme substrate (ES) complexes’ formation.

Prevents

The Inhibition of forming the Enzyme Substrate (ES) complex ________ the catalyzation of reactions and decreases the amount of product produced by a reaction.

Mercury and Cadmium

An example of poisonous substances that disable cofactors includes the heavy metals _______ replace zinc cofactors in some enzymes and inhibit their functioning.

Heme

An example of an enzyme Cofactor is the _____ portion of Hemoglobin. This Cofactor requires iron for its function and it is extremely important because it aids in oxygen binding to red blood cells in the blood.

Covalent bonds

Inhibition may be irreversible if the inhibitor attaches to __________

Weak bonds

Inhibition may be reversible if the inhibitor attaches to _________

Competitive Inhibitors

__________ are chemicals that resemble an enzyme’s normal substrate and compete with it for the active site. They block the active sites from the substrate.

Substrate Concentration

If Competitive Inhibitors are reversible, these inhibitors can be overcome by increased ___________

Non-Competitive Inhibitors

_________ are molecules that do not enter the enzyme’s active site but bind to another part of the enzyme molecule. The substrate is till able to access the active site, however, it alters the configuration of the enzyme so it is no longer fully functional.

Inhibitor

An _________ bonds to the enzyme and alters or destroys the enzymes activity.

Changes shape

When the inhibitor is bound, the active site ________ and the substrate no longer fits.

Reversible or Irreversible

Inhibition can be _________

Noncompetitive Inhibitor

A ___________ bonds to the enzyme, but not to the active site.

Competitive Inhibitor

A __________ has a shape and structure similar to the substrate, so it competes with the substrate for binding to the active site.