Name: enzyme helpers: metals, vitamins, and more
Uploaded: 2019-07-31T14:21:57.000Z
Duration: 1 min 27 s
Channel: JoVE

- In veel gevallen hebben enzymes extra moleculen nodig, cofactoren genaamd, om te functioneren. Deze helpermoleculen kunnen geclassificeerd worden als metaalionen of organische niet-proteïne moleculen. Bijvoorbeeld, tijdens de eerste stap van glycolyse bindt de cofactor magnesium aan ATP en spant de verbinding tussen twee van de fosfaatgroepen aan.

Deze actie laat de laatste fosfaatgroep toe om makkelijker los te laten door het enzyme hexokinase, en zo glucose om te zetten in glucose 6-fosfaat. Dus magnesium als cofactor bindt zich aan en verhoogt de efficiëntie van het ATP. Het andere subset van cofactoren, co-enzymes, zijn organische verbindingen, meestal afgeleiden van vitamines.

Bijvoorbeeld, vitamine C is een belangrijke co-enzyme bij de synthese van het proteïne collageen. Wanneer collageen bindt aan zijn enzyme hydroxylase, zal vitamine C zich aan het enzyme binden en een hydroxylgroep afstaan. Nu kan de gehydroliseerde hydroxylase helpen om de vorm van het collageen te veranderen naar zijn finale, triple helixstructuur, die essentieel is voor het instandhouden van belangrijke lichaamsweefsels.

cofactoren en co-enzymen

Cofactors and Coenzymes

Enzymen hebben extra componenten nodig voor een goede werking. Er zijn twee van dergelijke klassen moleculen: cofactoren en co-enzymen. Cofactoren zijn metaalionen en co-enzymen zijn niet-eiwit organische moleculen. Beide soorten helpermoleculen kunnen stevig aan het enzym gebonden zijn of alleen gebonden zijn wanneer het substraat bindt.

Cofactoren zijn aanwezig in ~30% van de volwassen eiwitten. Ze worden vaak opgenomen in een enzym terwijl het is gevouwen en zijn betrokken bij de katalytische activiteit van het enzym. Magnesium is een essentiële cofactor voor meer dan 300 enzymen in het menselijk lichaam, waaronder DNA-polymerase. In dit geval helpt het magnesiumion bij de vorming van de fosfodiesterbinding op de DNA-skelet. IJzer, koper, kobalt en mangaan zijn andere veel voorkomende cofactoren.

Veel vitamines zijn co-enzymen, omdat het niet-eiwitachtige, organische hulpmoleculen voor enzymen zijn. Biotine – een type B-vitamine – is bijvoorbeeld belangrijk in een verscheidenheid aan enzymen die kooldioxide van het ene molecuul naar het andere overbrengen. Biotine, vitamine A en andere vitamines moeten via onze voeding worden opgenomen, omdat ze niet door menselijke cellen kunnen worden aangemaakt.

Cofactoren en co-enzymen

Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions ...

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enzyme helpers: metals, vitamins, and more

Enzyme helpers are needed for many enzymes to work properly. These helpers fall into two groups: cofactors and coenzymes. Cofactors are metallic ions, while coenzymes are non-protein organic molecules. Both can be tightly bound to an enzyme or attach only when the substrate binds.

Cofactors are common in mature proteins, appearing in about 30% of them. They are often added as the enzyme folds and help with catalytic activity. Magnesium is one important cofactor, and it is needed by more than 300 enzymes in the human body, including DNA polymerase. In DNA polymerase, magnesium helps form the phosphodiester bond in the DNA backbone. Iron, copper, cobalt, and manganese are other common cofactors.

Many coenzymes come from vitamins. These organic helper molecules assist enzymes during reactions. Biotin, which is a B vitamin, helps several enzymes move carbon dioxide from one molecule to another. Vitamin A and other vitamins must come from the diet because human cells cannot make them.

Enzyme Helpers: Metals, Vitamins, and More

what is metabolism?

Metabolism, Energy, and Cell Reactions

Metabolism is the set of chemical reactions that happen in a cell. It includes anabolism, which builds molecules, and catabolism, which breaks them down. These reactions help cells manage energy and keep life processes running. Cells use metabolism to turn food into energy, make cell parts, and remove waste products. Food stores potential energy in the bonds between atoms. Catabolic pathways break large food molecules into smaller ones and release that energy. Anabolic pathways use that energy...

first law of thermodynamics

Energy Flow in a Food Web

Energy flow in a food web shows the First Law of Thermodynamics in action. Energy cannot be created or destroyed. It can only change form as it moves through living things and the environment. Sunlight is the starting point. Plants capture radiant energy from the sun during photosynthesis and turn it into chemical energy stored in complex carbohydrates. At the same time, oxygen is released into the atmosphere. Herbivores eat the plants and use those sugars during digestion. The energy is...

second law of thermodynamics

Entropy in Food Web Energy Flow

The Second Law of Thermodynamics explains why entropy increases as energy moves through a system. Entropy means the amount of disorder in a system. Each time energy is transferred or transformed, some energy is lost as unusable heat. That heat can raise the motion of nearby molecules for a short time and make the surroundings less ordered and more random. This idea also appears in a food web. Primary producers, such as plants, take in energy from the sun and make food. During this process,...

kinetic energy

Motion as a Source of Energy

Kinetic energy is the energy of motion. It appears when an object is moving and can do work or cause change. A waterfall is one clear example. Water behind a dam has potential energy, but when it rushes downward, that moving water has kinetic energy. When the water reaches the bottom and stops moving, its energy can become potential energy again. Kinetic energy also shows up in living systems. Plants absorb light particles, called photons, which move very fast and help create chemical energy...

potential energy

Stored Energy in Motion and Bonds

Stored energy in motion and bonds is called potential energy. It depends on the structure of an object or the position of matter in space. Raising a kettlebell changes its location and increases its potential energy. A stretched rubber band also stores potential energy, which can later change into kinetic energy. Chemical bonds between atoms hold another form of stored energy called chemical energy. These bonds involve attractive forces, and that energy can change into other forms during a...

free energy

Gibbs Free Energy in Chemical Reactions

Gibbs free energy is a measure of useful energy that can be taken from a chemical reaction to do work. It is written as G and named for scientist Gibbs, who discovered it. This energy is what remains after entropy is considered. A reaction can either take in energy or release it. Reactions that absorb energy are called endergonic reactions. Reactions that release energy are called exergonic reactions. The direction of energy flow helps show which type of reaction is happening. Plants carry...

activation energy

How Catalysts Lower Reaction Barriers

Activation energy is the minimum energy a chemical reaction needs to keep going. When the activation energy is higher, the reaction usually happens more slowly. Adding heat can speed the reaction because molecules move faster and collide more often. As reactants collide, bonds break and the reaction moves through an uphill phase. That step creates the transition state, which is an unstable, high-energy state of the reactants. After that, new bonds form, products appear, and free energy is...

hydrolysis of atp

ATP Breakdown and Energy Release

ATP breakdown releases energy for cell work. Adenosine triphosphate, or ATP, can lose one or two phosphate groups when water is added. This hydrolysis reaction is exergonic, which means it releases energy that the cell can use. When one phosphate group is removed, ATP becomes ADP, or adenosine diphosphate. Inorganic phosphate is also released. ADP can then be hydrolyzed again to form AMP, or adenosine monophosphate, after a second phosphate group is removed. ATP has a clear structure. It is...

phosphorylation

Phosphorylation and Protein Control

Phosphorylation helps control how proteins work in cells. It is the addition or removal of phosphate groups, and it is the most common chemical change that regulates cellular processes. These changes can alter a protein’s structure, activity, stability, location inside the cell, and interactions with other proteins. During phosphorylation, protein kinases move the terminal phosphate group from ATP to a specific amino acid side chain on a target protein. The amino acids most often...

induced-fit model

How Enzymes Adjust to Their Substrates

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enzyme kinetics

Substrate Effects on Enzyme Rates

Enzyme kinetics examines how enzymes change the rate of a reaction. Enzymes speed reactions by lowering the activation energy of the reactants. The reaction rate is the speed at which an enzyme turns reactants into products, and it can be affected by several factors, including the number of available reactants. Scientists often study enzyme kinetics in a test tube with a fixed amount of enzyme. When more substrate, or reactant, is added, the reaction rate increases because the enzyme can make...

enzyme inhibition

Competitive vs Noncompetitive Inhibitors

Enzyme inhibitors are molecules that reduce enzyme activity by binding to enzymes. Cells use these inhibitors to help regulate normal enzyme function. Drugs and toxins can also block enzymes and change how they work. Some inhibitors bind at the active site, which is the part of the enzyme where the substrate normally fits. Competitive inhibitors do this by occupying the active site and preventing the substrate from binding. If the substrate concentration becomes high enough, it can outcompete...

feedback inhibition

How Cells Control Product Buildup

Cells use enzymes to run biochemical reactions and make the products they need. These reactions are happening constantly, and enzymes speed them up so they happen fast enough to matter. Enzyme activity also has to be regulated. Cells need the right amounts of starting materials, intermediate metabolites, and final products. If these substances build up too much or drop too low, the cell can be harmed. That is why cells use control systems to keep metabolic levels balanced. One important...

allosteric regulation

Allosteric Control of Enzyme Speed

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cofactors and coenzymes

Enzyme helpers are needed for many enzymes to work properly. These helpers fall into two groups: cofactors and coenzymes. Cofactors are metallic ions, while coenzymes are non-protein organic molecules. Both can be tightly bound to an enzyme or attach only when the substrate binds. Cofactors are common in mature proteins, appearing in about 30% of them. They are often added as the enzyme folds and help with catalytic activity. Magnesium is one important cofactor, and it is needed by more than...

key terms and concepts

Learn how cofactors and coenzymes help enzymes work, from magnesium in DNA polymerase to biotin and other vitamin-based helpers.

Enzyme Helpers: Metals, Vitamins, and More | JoVE K12

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Enzyme Helpers: Metals, Vitamins, and More

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