Enzymes and Biocatalysis Quiz

Enzymes and Biocatalysis

• Enzymes are protein molecules found in all living things

• They speed up chemical reactions, often millions of times faster

• Enzymes aid digestion, metabolism, and waste elimination

• Enzymes are crucial in muscle contraction

• Enzymes play a vital role in food production (e.g., dough making)

• They can be extracted from plants, animals, or created through microbial fermentation

• Enzymes are the body's essential workforce for daily activities and survival

• Life depends on a series of chemical reactions, many too slow without enzymes

• Enzymes serve as catalysts

• Enzymes are essential in many manufacturing processes and consumer products

• Many diseases are linked to abnormal enzyme activity

• Pharmaceuticals often target enzymes for therapeutic purposes (inhibitors)

• Living organisms synthesize enzymes (animals, plants, microorganisms).

• This process involves transcription and translation.

• Transcription in the nucleus creates mRNA from the DNA segment coding for a specific protein using RNA polymerase

• mRNA is transported into the cytoplasm to undergo translation -Translation in the ribosome uses the mRNA transcript to create proteins in the correct amino acid sequence.

• DNA holds genetic information for constructing proteins

• The nucleotide sequence of a gene directs the creation of the corresponding protein’s amino acid sequence.

• Four structures of proteins derived from the amino acid sequence: primary, secondary, tertiary, quaternary.

• Enzymes, being proteins, are often at the quaternary level of protein structure.

• Enzymes achieve their final form through protein folding processes.

• Specific regions on enzymes, called active sites, bind to substrates and catalyze the conversion of substrates into products.

• Some enzymes require additional non-protein molecules (cofactors) for activity,

• Cofactors can be inorganic ions (e.g., metal ions) or small organic molecules (coenzymes)

• Metal ions (e.g., Mg2+, Cu2+, Fe2+, Fe3+, Ca2+, Zn2+, Mn2+, Ni2+ etc.) are often bound to amino acid side chains.

• Metal ions perform roles such as electron transfer and substrate stabilization in the active site

• Metalloenzymes result from metal ions tightly bound to the enzyme molecule

• Coenzymes are small organic molecules either loosely or tightly bound to the enzyme molecule.

• They aid in preparing the active site for substrate binding and/or participate in catalysis.

• Coenzymes aren't destroyed during reactions and are critical in several biochemical reactions.

• A coenzyme or metal ion covalently bound to an enzyme is a prosthetic group. -Apoenzymes are the protein portions of enzymes without their necessary prosthetic groups

• Holoenzymes are catalytically active enzymes with their cofactors

• A zymogen or proenzyme is an inactive precursor form of an enzyme.

• An activator is a substance that enhances an enzyme's reaction rate.

• Coenzymes are metabolically active forms of vitamins

• Vitamins are essential organic compounds in small quantities for metabolism, normal growth, and health; they can not be efficiently synthesized by the body

• Some body can synthesize a portion of vitamins such as vitamin D and niacin.

• Vitamins are classified as either fat-soluble or water-soluble, with different roles in the body

• Many coenzymes originate from water-soluble vitamins

• Examples of vitamins are Thiamin, Riboflavin, Niacin

• Common coenzyme forms of Riboflavin are FMN, FAD

• FMN and FAD are prosthetic groups of oxidoreductase enzymes in several metabolic pathways (especially fatty acid degradation)

• Niacin forms coenzymes, NAD+ and NADP+.

• NAD+ and NADPH are involved in oxidation-reduction reactions in carbohydrate, lipid, and protein metabolism

• Examples of Enzyme Reactions involving coenzymes include: -- Glyceraldehyde 3-Phosphate Dehydrogenase, Lactate Dehydrogenase and Pyruvate Dehydrogenase Complex

• Enzymes have specific, defined names based upon the reaction they catalyse and/or the substrate, and end with -ase.

• The IUBMB created an international commission to standardize enzyme nomenclature including an EC number.

• EC number is used to classify enzymes. -Enzymes are highly specific and typically interact with only one or a few types of substrates

• There are different types of specificity (absolute, group, relative group).

• Different models explain enzyme specificity and how an enzyme, and substrate interact including the lock-and-key model and the induced-fit model

• Enzymes lower the activation energy of a reaction.

• The activation energy of the catalyzed enzyme reaction lowers the required energy for enzymes to catalyze reactions.

• Factors that affect enzyme activity include temperature, pH and substrate/enzyme concentrations.

Test your knowledge on enzymes and their role as biocatalysts in living organisms. This quiz covers specific functions, importance in chemical reactions, and their applications in various industries. Understand how enzymes are synthesized and their impact on health and production processes.