Vitamins and Enzymes Overview

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to Lesson

Podcast

Play an AI-generated podcast conversation about this lesson
Download our mobile app to listen on the go
Get App

Questions and Answers

What is the role of NAD+ primarily associated with?

  • Synthesis of carbohydrates
  • Biosynthesis of lipids
  • Catabolic reactions (correct)
  • Anabolic reactions

How is FAD reduced to FADH2?

  • By donating an electron and a proton
  • By taking up a proton and two electrons (correct)
  • By accepting two protons only
  • By undergoing hydrolysis

Which vitamin is a precursor for Thiamine Pyrophosphate (TPP)?

  • Vitamin C
  • Vitamin B1 (correct)
  • Vitamin B2
  • Vitamin B6

What type of reactions is Coenzyme A (CoA) primarily involved in?

<p>Acyl-group transfer reactions (C)</p> Signup and view all the answers

What is a key characteristic of FAD and FMN as prosthetic groups?

<p>They are tightly bound, usually noncovalently (B)</p> Signup and view all the answers

What is the primary function of NADPH in biological systems?

<p>Reducing agent in biosynthetic reactions (D)</p> Signup and view all the answers

Which type of reaction is primarily catalyzed by enzymes utilizing Pyridoxal Phosphate (PLP)?

<p>Amino acid rearrangements (B)</p> Signup and view all the answers

Which enzyme class is associated with the transfer of functional groups to water?

<p>Hydrolases (A)</p> Signup and view all the answers

What is the general function of cofactors in enzymatic reactions?

<p>To convert inactive apoenzymes to active holoenzymes (A)</p> Signup and view all the answers

Which of the following classes of enzymes involves the addition of groups to double bonds?

<p>Lyases (A)</p> Signup and view all the answers

What is the best description of the reaction catalyzed by hexokinase?

<p>Phosphorylation of glucose using ATP (B)</p> Signup and view all the answers

Which statement about enzymes is true?

<p>They do not affect equilibrium concentrations of substrates and products. (D)</p> Signup and view all the answers

What is the role of absolute requirement for added metal ions in metal-activated enzymes?

<p>They are essential for achieving full catalytic activity. (C)</p> Signup and view all the answers

What type of reaction does the enzyme class transferases primarily catalyze?

<p>Group transfer reactions (D)</p> Signup and view all the answers

Which enzyme class includes enzymes that catalyze the formation of C-C, C-S, C-O, and C-N bonds?

<p>Ligases (B)</p> Signup and view all the answers

Which metal ions are most commonly found in metalloenzymes?

<p>Iron and zinc (D)</p> Signup and view all the answers

What is a characteristic feature of cosubstrates compared to prosthetic groups?

<p>They are substrates in enzyme-catalyzed reactions. (D)</p> Signup and view all the answers

Why do animals, including humans, require external sources of coenzymes?

<p>They lack the ability to synthesize certain coenzymes. (A)</p> Signup and view all the answers

What is the purpose of the recommended dietary allowance (RDA) for vitamins?

<p>To define the amount of vitamins needed to prevent deficiency-related illnesses. (D)</p> Signup and view all the answers

Which of the following is NOT a recognized cause of nutritional-deficiency diseases?

<p>An excess of dietary fiber (D)</p> Signup and view all the answers

Which vitamin can be synthesized endogenously from 7-dehydrocholesterol?

<p>Vitamin D (A)</p> Signup and view all the answers

What units are used to measure vitamin concentration in the diet?

<p>mcg (µg) and IU (D)</p> Signup and view all the answers

During which of the following conditions might a nutritional-deficiency disease occur?

<p>Pregnancy and lactation periods (D)</p> Signup and view all the answers

Which type of organisms are the ultimate sources of vitamins for mammals?

<p>Microorganisms and plants (D)</p> Signup and view all the answers

What can be considered a provitamin?

<p>A compound that the body converts into a vitamin (A)</p> Signup and view all the answers

Which vitamin deficiency is primarily associated with neural tube defects in developing embryos?

<p>Vitamin B9 (D)</p> Signup and view all the answers

What is the primary cofactor form of Vitamin B9 in the body?

<p>Tetrahydrofolate (A)</p> Signup and view all the answers

Which of the following sources is NOT recommended for acquiring Vitamin B12?

<p>Legumes (B)</p> Signup and view all the answers

What process facilitates the absorption of lipid vitamins in the intestine?

<p>Interaction with bile salts (B)</p> Signup and view all the answers

What deficiency leads to pernicious anemia?

<p>Vitamin B12 deficiency (A)</p> Signup and view all the answers

Which function is NOT associated with Vitamin C?

<p>Coenzyme in fatty acid metabolism (C)</p> Signup and view all the answers

What is the Recommended Daily Allowance (RDA) for Vitamin B9?

<p>400 µg (A)</p> Signup and view all the answers

What binds Vitamin B12 in the ileum for cellular uptake?

<p>Intrinsic factor (A)</p> Signup and view all the answers

Which type of anemia results from Vitamin B9 deficiency?

<p>Megaloblastic anemia (D)</p> Signup and view all the answers

What role does Vitamin C play in the body?

<p>Facilitates collagen hydroxylation (A)</p> Signup and view all the answers

What is one of the advanced symptoms associated with the Wernicke-Korsakoff syndrome?

<p>Mental convulsion (B)</p> Signup and view all the answers

Which vitamin's deficiency is characterized by Pellagra, known for its three 'D's?

<p>Vitamin B3 (A)</p> Signup and view all the answers

Which dietary source is rich in Riboflavin (Vitamin B2)?

<p>Eggs (D)</p> Signup and view all the answers

What is the recommended daily allowance of Vitamin B6 (Pyridoxine)?

<p>1.3 mg (C)</p> Signup and view all the answers

Which cofactor is associated with Vitamin B5 (Pantothenic acid)?

<p>Coenzyme A (C)</p> Signup and view all the answers

What are the symptoms of riboflavin deficiency in the context of hypothyroidism?

<p>Inflammation of the mouth and tongue (B)</p> Signup and view all the answers

What is a significant effect of alcohol on the body's vitamin metabolism?

<p>Inhibits vitamin intake and metabolism (B)</p> Signup and view all the answers

Which of the following is a dietary source of Vitamin B7 (Biotin)?

<p>Natural products and synthesized by bacteria (C)</p> Signup and view all the answers

What is the primary role of TPP in the body?

<p>Cofactor involved in neurotransmission (A)</p> Signup and view all the answers

Which condition is indicated by the 'necklace' lesions on the skin?

<p>Pellagra due to niacin deficiency (A)</p> Signup and view all the answers

Flashcards

Transferases

A group of enzymes that catalyze the transfer of functional groups from one molecule to another.

Active Site

The specific site on an enzyme where the substrate binds and the reaction occurs.

Substrate

A molecule that binds to the enzyme's active site and is acted upon by the enzyme.

Enzymes and Activation Energy

Enzymes lower the activation energy of a reaction, but they do not affect the equilibrium constants or the overall free energy change.

Signup and view all the flashcards

Apoenzyme

The inactive form of an enzyme that requires a cofactor to become active.

Signup and view all the flashcards

Cofactor

A non-protein molecule that assists an enzyme in its catalytic activity.

Signup and view all the flashcards

Holoenzyme

The complete and active form of an enzyme, consisting of an apoenzyme and a cofactor.

Signup and view all the flashcards

Essential Ions

Metal ions that are essential for the activity of many enzymes.

Signup and view all the flashcards

Metalloenzymes

Enzymes containing a tightly bound metal ion within their active site. These ions often play a crucial role in catalysis, influencing the enzyme's activity.

Signup and view all the flashcards

Cosubstrates

A key component involved in enzyme-catalyzed reactions. They are not permanently bound to the enzyme.

Signup and view all the flashcards

Prosthetic Group

A type of coenzyme permanently bound to an enzyme's active site, indispensable for its function.

Signup and view all the flashcards

Avitaminosis

A nutritional deficiency disease arising from the lack of a specific vitamin in an organism's diet.

Signup and view all the flashcards

Recommended Dietary Allowance (RDA)

The recommended daily intake of a vitamin crucial for maintaining optimal health and preventing deficiency.

Signup and view all the flashcards

Provitamin

A precursor form of a vitamin found in food that is often converted into its active form within the body.

Signup and view all the flashcards

Endogenous Vitamin Synthesis

The ability of certain organisms to synthesize vitamins internally, like Vitamin D from the sun and K from gut bacteria.

Signup and view all the flashcards

Vitamins

The essential micronutrients required by animals, including humans, that they cannot synthesize themselves and must obtain from external sources.

Signup and view all the flashcards

Iron

A common metal ion found in metalloenzymes, crucial for diverse biological functions.

Signup and view all the flashcards

Zinc

A common metal ion found in metalloenzymes, playing a vital role in various enzymatic reactions.

Signup and view all the flashcards

What are NAD+ and NADP+?

NAD+ and NADP+ are coenzymes that act as electron carriers in many metabolic reactions. They accept two electrons and a proton, becoming reduced to NADH and NADPH, respectively. Their oxidation-reduction reactions are essential for energy production and biosynthesis.

Signup and view all the flashcards

What is the primary role of NADH?

NADH is primarily used in catabolic reactions, where it carries electrons from the breakdown of fuels (like glucose) to the electron transport chain, generating ATP. This process contributes to energy production in our cells.

Signup and view all the flashcards

What is the primary role of NADPH?

NADPH is mainly used in anabolic reactions, where it provides reducing power for biosynthesis pathways. It's essential for building up molecules like fatty acids, cholesterol, and nucleotides.

Signup and view all the flashcards

What are FAD and FMN?

FAD and FMN are coenzymes derived from riboflavin (vitamin B2). They act as electron carriers in redox reactions, accepting two electrons and two protons, becoming reduced to FADH2 and FMNH2, respectively.

Signup and view all the flashcards

What is Coenzyme A (CoA) and its role?

CoA is a coenzyme involved in acyl-group transfer reactions. It plays a crucial role in metabolism, particularly in the oxidation of fuel molecules and the biosynthesis of carbohydrates and lipids.

Signup and view all the flashcards

What is Thiamine Pyrophosphate (TPP) and its role?

TPP is a coenzyme derived from thiamine (vitamin B1). It is essential for many decarboxylase enzymes, which catalyze the removal of carbon dioxide from molecules. It is also involved in the oxidative decarboxylation of alpha-keto acids.

Signup and view all the flashcards

What is Pyridoxal Phosphate (PLP) and its role?

PLP is a coenzyme derived from pyridoxal phosphate (vitamin B6). It is a prosthetic group for many enzymes involved in amino acid metabolism, including transaminases, which catalyze the transfer of amino groups.

Signup and view all the flashcards

What is Wernicke-Korsakoff Syndrome?

A deficiency of Thiamine (B1) can lead to the Wernicke-Korsakoff syndrome, characterized by neurological problems like mental confusion, ataxia (loss of coordination), and memory impairment.

Signup and view all the flashcards

What is Thiamine (B1) essential for?

Thiamine (B1) plays a crucial role in the metabolism of carbohydrates and nerve function. It's essential for converting glucose into energy.

Signup and view all the flashcards

What are the active coenzymes of Riboflavin (B2)?

Riboflavin (B2) is converted into FMN and FAD, important coenzymes involved in various metabolic reactions and energy production.

Signup and view all the flashcards

What are the symptoms of Riboflavin (B2) deficiency?

Riboflavin (B2) deficiency can cause glossitis (inflammation of the tongue) and stomatitis (inflammation of the mouth), indicating potential issues with the digestive tract and overall health.

Signup and view all the flashcards

What are the active coenzymes of Niacin (B3)?

Niacin (B3) is converted into NAD and NADP, important coenzymes crucial for redox reactions (electron transfer) essential for energy production.

Signup and view all the flashcards

What is Pellagra, and what causes it?

A deficiency of Niacin (B3) can cause Pellagra, a condition characterized by the ‘three Ds’: diarrhea, dermatitis, and dementia.

Signup and view all the flashcards

What is Pantothenic acid (B5) converted into, and what is its function?

Pantothenic acid (B5) is converted into Coenzyme A, which plays a vital role in various metabolic processes, including the breakdown of carbohydrates, fats, and proteins.

Signup and view all the flashcards

What is Pyridoxine (B6) essential for?

Pyridoxine (B6) is essential for the synthesis of neurotransmitters, which are crucial for communication between nerve cells.

Signup and view all the flashcards

What is Biotin (B7) involved in?

Biotin (B7) is a coenzyme of carboxylase enzymes, involved in the metabolism of carbohydrates and the synthesis of fatty acids.

Signup and view all the flashcards

What are the symptoms of Biotin (B7) deficiency?

Biotin (B7) deficiency can lead to neurological symptoms in adults, including depression, highlighting the importance of B7 in mental health.

Signup and view all the flashcards

What is the function of folate (vitamin B9)?

A coenzyme required for a variety of metabolic reactions including DNA synthesis, amino acid metabolism, and red blood cell formation.

Signup and view all the flashcards

What is a major consequence of folate deficiency during pregnancy?

A deficiency in folate can lead to neural tube defects, a serious birth defect that can happen in the developing embryo.

Signup and view all the flashcards

What is the function of 5'-deoxyadenosylcobalamin (cobalamin)?

This form of vitamin B12 is required for the synthesis of myelin, the protective sheath around nerve fibers.

Signup and view all the flashcards

What is intrinsic factor (IF) and what is its role in vitamin B12 absorption?

It is secreted by the parietal cells of the stomach and binds to vitamin B12 in the ileum.

Signup and view all the flashcards

What is megaloblastic anemia and what causes it?

This type of anemia is characterized by the production of large, immature red blood cells.

Signup and view all the flashcards

What is the main function of vitamin C (ascorbic acid)?

Vitamin C acts as a reducing agent during the hydroxylation of collagen, a key protein for connective tissues.

Signup and view all the flashcards

What causes scurvy and what are its symptoms?

This deficiency disease causes various health problems including fatigue, poor wound healing, and bleeding gums.

Signup and view all the flashcards

Where can you find vitamin C in your diet?

Dietary sources of vitamin C include fruits and vegetables such as tomatoes, potatoes, and leafy greens.

Signup and view all the flashcards

What are the structural characteristics of lipid-soluble vitamins (A, D, E, and K)?

They have a hydrophobic structure consisting of rings and long aliphatic side chains.

Signup and view all the flashcards

How are lipid-soluble vitamins absorbed in the digestive system?

After digestion, they are packaged as micelles with bile salts and transported to the intestinal cells.

Signup and view all the flashcards

Study Notes

Vitamins and Cofactors

  • Vitamins are essential compounds that animals often obtain from plants or microorganisms
  • Mammals and carnivorous animals might obtain vitamins from eating meat
  • Some vitamins are provitamins, meaning they need to be activated in the body
  • Some vitamins can be synthesized endogenously
  • Recommended daily allowances (RDAs) for vitamins are determined by international health organizations and vary based on age and gender

Enzymes

  • Organisms need enzymes to efficiently and selectively catalyze chemical reactions.
  • Enzymes are central to all biochemical processes
  • Enzymes are highly specific for their substrates
  • Enzymes accelerate chemical reactions significantly
  • Enzymes typically function at mild temperature and pH in aqueous solutions
  • All enzymes are proteins, except for a small group of catalytic RNA molecules (ribozymes)
  • Their catalytic activity relies on their native protein conformation
  • Molecular weights of enzymes range from 12,000 to more than one million Daltons
  • Some enzymes only require amino acid residues for activity, while others need additional cofactors

Cofactors

  • Cofactors are inorganic ions (e.g., Fe²⁺, Mg²⁺, Mn²⁺, Zn²⁺), or complex organic/metalloorganic molecules (coenzymes)
  • Coenzymes act as transient carriers of functional groups
  • A tightly bound coenzyme or metal ion is called a prosthetic group
  • The complete, active enzyme with its cofactors is called a holoenzyme
  • The protein part of the enzyme without the cofactor is called an apoenzyme or apoprotein

Enzyme Classification

  • Enzymes are categorized based on the reactions they catalyze
  • Many enzymes are named by adding "-ase" to the substrate name or a descriptor of their activity
  • Examples include: Urease (hydrolysis of urea); DNA polymerase (polymerization of nucleotides to form DNA); Pepsin (digestion); Lysozyme (lyse bacterial walls)
  • Enzymes may have different names or there may be different enzymes with the same name.
  • Enzymes are grouped into classes. An international classification system exists.

Essential lons

  • More than 25% of known enzymes require metal ions for full activity
  • Some enzymes have an absolute requirement for specific metal ions while others are stimulated by added metal ions
  • Examples of essential ions for enzyme activity include Mg2+ and Ca2+ for many metabolic reactions and K+ for some enzymes

Metalloenzymes

  • Metalloenzymes contain firmly bound metal ions at active sites
  • Common metal ions include iron (Fe) and zinc (Zn), with less common use of copper (Cu) and cobalt (Co)
  • Examples include carbonic anhydrase (erythrocytes) that catalyzes CO₂ + H₂O → H⁺ + HCO₃⁻

Inorganic elements

  • Many inorganic elements serve as cofactors for enzymes.
  • Several examples include Cu²⁺, Fe²⁺/Fe³⁺, K⁺, Mg²⁺, Mn²⁺, Mo, Ni²⁺, Se, and Zn²⁺, each with specific enzyme functions

Coenzymes

  • Cosubstrates: temporarily bind and dissociate from the enzyme during the reaction.
  • Prosthetic groups: tightly bind to the enzyme and remain associated throughout the reaction.
  • Animals require a source of coenzymes or precursors to survive because they cannot synthesize all of them.
  • Prokaryotes, protists, fungi and plants are capable of synthesizing coenzymes from simple precursors. But animals (including humans) cannot.

Structure and Function of Vitamins

  • Vertebrates typically rely on other organisms for vitamin supply.
  • Most vitamin sources are plants or microorganisms even though carnivorous animals can obtain them from meat.
  • Some vitamins are provitamins, which need to be activated in the body. .
  • Some vitamins can be synthesized endogenously by the body. This is true for vitamin D from 7-dehydrocholesterol and vitamin K from intestinal flora

RDA for Vitamins

  • RDAs or DRIs are defined as the amount of a vitamin needed to protect the body against illness
  • They differ based on a person's age and gender.
  • Units for vitamin concentrations are mcg (μg) and International Unit (IU)

Nutritional deficiency Diseases (Avitaminoses)

  • A deficiency of a vitamin or absence of vitamins in an animal's diet can result in nutritional or vitamin deficiency diseases
  • Some examples of vitamin-deficiency diseases include scurvy (vitamin C deficiency); pellagra (niacin deficiency); growth retardation (riboflavin deficiency); dermatitis (pantothenate deficiency), beri beri (thiamine deficiency)

Vitamin Classification

  • Water-soluble vitamins are excreted in urine, do not cause hypervitaminosis, and are often heat sensitive (except B12).
  • Fat-soluble vitamins are absorbed with fats, are stored in the body (and an overdose can cause toxicity), and are not as sensitive to heat.

Specific Vitamins

  • Detailed information about individual vitamins (B1, B2, B3, B5, B6, biotin, B9, B12, vitamin C, A, D, E, K) including their sources, functions, cofactors, and deficiencies are presented in the provided text.

How Enzymes Work

  • Active site: The location where the enzyme-catalyzed reaction occurs
  • Substrate: The molecule acted upon in the active site
  • Enzymes reduce the activation energy of a reaction (but do not change the overall free energy change or the equilibrium concentrations).

Cofactor Requirements

  • Cofactors are often essential for converting inactive apoenzymes to active holoenzymes.

Nucleotide-sugar coenzymes

  • Provide detailed examples of nucleotide-sugar coenzymes, such as UDP-glucose, and their involvement in biosynthetic reactions, particularly glycogen synthesis.

Other coenzymes

  • Detailed information is presented in the provided text about various coenzymes like NAD+, NADP+, FAD, FMN, CoA, lipoamide, Ubiquinone (Coenzyme Q). This information includes sources, functions, and the reactions they are involved in

Studying That Suits You

Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

Quiz Team

Related Documents

More Like This

Enzymes and Vitamins Quiz
71 questions
Enzymes and Vitamins Quiz
37 questions

Enzymes and Vitamins Quiz

SubstantiveKineticArt avatar
SubstantiveKineticArt
Biochemistry Quiz: Enzymes and Metabolism
81 questions
Enzymes, Vitamins, and Biological Molecules
43 questions
Use Quizgecko on...
Browser
Browser