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

Em muitos casos, as enzimas exigem moléculas adicionais chamadas cofatores para funcionar. Estas as moléculas ajudantes podem ser classificadas como iões metálicos ou moléculas orgânicas não proteicas. Por exemplo, durante a primeira etapa da glicólise, o cofator magnésio liga-se ao ATP, estreitando o vínculo entre dois dos grupos fosfatos.Esta ação permite que o último grupo fosfato seja liberado mais facilmente pela enzima hexoquinase, transformando glicose em glicose 6-fosfato. Portanto, o magnésio, como um cofator, liga e aumenta a eficiência do ATP. O outro subconjunto de cofatores coenzimas são compostos orgânicos, geralmente derivados de vitaminas.Por exemplo, a vitamina C é uma coenzima importante na síntese de da proteína de colágeno. Quando uma hidroxilase liga-se ao colágeno, a vitamina C facilita a hidroxilação de resíduos no colágeno. Com a ajuda de vitamina C, a hidroxilase promove a mudança na forma do colágeno à sua estrutura helicoidal tripla final, que é essencial para a manutenção de importantes tecidos do corpo.

"Estrutura e função das carboxilases dependentes de biotina." Ciências da Vida Celular e Molecular 70, nº 5 (2013): 863-891. [<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3508090/">Fonte</a>]

Yang, Wei, Jae Young Lee e Marcin Nowotny. "Fazendo e quebrando ácidos nucléicos: catálise de dois íons Mg2 + e especificidade do substrato." Célula Molecular 22, nº 1 (2006): 5-13. [<a href="https://doi.org/10.1016/j.molcel.2006.03.013">Fonte</a>]

cofatores e coenzimas

Cofactors and Coenzymes

As enzimas requerem componentes adicionais para uma função adequada. Existem duas dessas classes de moléculas: cofatores e coenzimas. Cofatores são iões metálicos e coenzimas são moléculas orgânicas não-proteicas. Ambos os tipos de moléculas auxiliares podem estar firmemente ligados à enzima ou ligados apenas quando o substrato se liga.
 
 Os cofatores estão presentes em ~30% das proteínas maduras. Eles são frequentemente incorporados em uma enzima à medida que ela é dobrada e estão envolvidos na atividade catalítica da enzima. O magnésio é um cofator essencial para mais de 300 enzimas no corpo humano, incluindo a DNA polimerase. Neste caso, o ião magnésio auxilia na formação da ligação fosfodiéster no esqueleto do DNA. Ferro, cobre, cobalto e manganês são outros cofatores comuns.
 
 Muitas vitaminas são coenzimas, uma vez que são moléculas auxiliares orgânicas, não proteicas para enzimas. Por exemplo, a biotina—um tipo de vitamina B—é importante em uma variedade de enzimas que transferem dióxido de carbono de uma molécula para outra.  Biotina, vitamina A e outras vitaminas devem ser ingeridas na nossa dieta, pois não podem ser produzidas por células humanas.

Cofatores e Coenzimas

As enzimas requerem componentes adicionais para o funcionamento adequado. Existem duas dessas classes de moléculas: cofatores e coenzimas. Os cofatores são íons metálicos ...

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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

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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

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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

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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

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induced-fit model

How Enzymes Adjust to Their Substrates

Enzymes speed up many chemical reactions in cells. They are biological catalysts, so they increase reaction speed without being consumed or permanently changed. They do this by lowering the activation energy needed to turn reactants into products. Enzymes are proteins that usually work by binding to a substrate, which is the reactant molecule they act on. They show substrate specificity, meaning they bind only certain substrates. This specificity depends mainly on the shape and chemical...

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

Allosteric control changes enzyme speed when a molecule binds to a site other than the active site. That alternate binding spot is called an allosteric site. An enzyme can have more than one allosteric site. This type of control can raise or lower enzyme activity. Many enzymes with allosteric control are metabolic enzymes. They help with the breakdown or the building of specific molecules in cells. In allosteric inhibition, the effector molecule causes a shape change that lowers the enzyme's...

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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