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Energy metabolism basics

Energy metabolism basics

Journal Energy metabolism basics Biosciences. For example, Energy metabolism basics are proteins and Enwrgy job is to metaolism chemical reactions. The Two Empires and Three Domains of Life in the Postgenomic Age. Glucose molecules can also be combined with and converted into other types of sugars. The nitrogen is incorporated into urea and then removed in the urine.

Energy metabolism basics -

Watch an animation of the move from free energy to transition state of the reaction. A substance that helps a chemical reaction to occur is called a catalyst, and the molecules that catalyze biochemical reactions are called enzymes.

Most enzymes are proteins and perform the critical task of lowering the activation energies of chemical reactions inside the cell. Most of the reactions critical to a living cell happen too slowly at normal temperatures to be of any use to the cell.

Without enzymes to speed up these reactions , life could not persist. Enzymes do this by binding to the reactant molecules and holding them in such a way as to make the chemical bond-breaking and -forming processes take place more easily.

It is important to remember that enzymes do not change whether a reaction is exergonic spontaneous or endergonic. This is because they do not change the free energy of the reactants or products. They only reduce the activation energy required for the reaction to go forward Figure 4.

In addition, an enzyme itself is unchanged by the reaction it catalyzes. Once one reaction has been catalyzed, the enzyme is able to participate in other reactions. There may be one or more substrates, depending on the particular chemical reaction.

In some reactions, a single reactant substrate is broken down into multiple products. In others, two substrates may come together to create one larger molecule. Two reactants might also enter a reaction and both become modified, but they leave the reaction as two products.

Since enzymes are proteins, there is a unique combination of amino acid side chains within the active site. Each side chain is characterized by different properties. They can be large or small, weakly acidic or basic, hydrophilic or hydrophobic, positively or negatively charged, or neutral.

The unique combination of side chains creates a very specific chemical environment within the active site. This specific environment is suited to bind to one specific chemical substrate or substrates. Active sites are subject to influences of the local environment.

Increasing the environmental temperature generally increases reaction rates, enzyme-catalyzed or otherwise. However, temperatures outside of an optimal range reduce the rate at which an enzyme catalyzes a reaction.

Hot temperatures will eventually cause enzymes to denature, an irreversible change in the three-dimensional shape and therefore the function of the enzyme. Enzymes are also suited to function best within a certain pH and salt concentration range, and, as with temperature, extreme pH, and salt concentrations can cause enzymes to denature.

This model asserted that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a model called induced fit Figure 4. The induced-fit model expands on the lock-and-key model by describing a more dynamic binding between enzyme and substrate.

View an animation of induced fit. When an enzyme binds its substrate, an enzyme-substrate complex is formed. This complex lowers the activation energy of the reaction and promotes its rapid progression in one of multiple possible ways.

On a basic level, enzymes promote chemical reactions that involve more than one substrate by bringing the substrates together in an optimal orientation for reaction. Another way in which enzymes promote the reaction of their substrates is by creating an optimal environment within the active site for the reaction to occur.

The enzyme-substrate complex can also lower activation energy by compromising the bond structure so that it is easier to break. Finally, enzymes can also lower activation energies by taking part in the chemical reaction itself. In these cases, it is important to remember that the enzyme will always return to its original state by the completion of the reaction.

One of the hallmark properties of enzymes is that they remain ultimately unchanged by the reactions they catalyze. After an enzyme has catalyzed a reaction, it releases its product s and can catalyze a new reaction.

However, a variety of mechanisms ensures that this does not happen. Cellular needs and conditions constantly vary from cell to cell, and change within individual cells over time.

The required enzymes of stomach cells differ from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive organ cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal.

As these cellular demands and conditions vary, so must the amounts and functionality of different enzymes. Since the rates of biochemical reactions are controlled by activation energy, and enzymes lower and determine activation energies for chemical reactions, the relative amounts and functioning of the variety of enzymes within a cell ultimately determine which reactions will proceed and at what rates.

This determination is tightly controlled in cells. In certain cellular environments, enzyme activity is partly controlled by environmental factors like pH, temperature, salt concentration, and, in some cases, cofactors or coenzymes.

Enzymes can also be regulated in ways that either promote or reduce enzyme activity. There are many kinds of molecules that inhibit or promote enzyme function, and various mechanisms by which they do so.

In some cases of enzyme inhibition , an inhibitor molecule is similar enough to a substrate that it can bind to the active site and simply block the substrate from binding. When this happens, the enzyme is inhibited through competitive inhibition , because an inhibitor molecule competes with the substrate for binding to the active site.

On the other hand, in noncompetitive inhibition , an inhibitor molecule binds to the enzyme in a location other than the active site, called an allosteric site , but still manages to block substrate binding to the active site.

Some inhibitor molecules bind to enzymes in a location where their binding induces a conformational change that reduces the affinity of the enzyme for its substrate. This type of inhibition is called allosteric inhibition Figure 4. Most allosterically regulated enzymes are made up of more than one polypeptide, meaning that they have more than one protein subunit.

When an allosteric inhibitor binds to a region on an enzyme, all active sites on the protein subunits are changed slightly such that they bind their substrates with less efficiency.

There are allosteric activators as well as inhibitors. Plants cannot run or hide from their predators and have evolved many strategies to deter those who would eat them.

Think of thorns, irritants and secondary metabolites: these are compounds that do not directly help the plant grow, but are made specifically to keep predators away.

Secondary metabolites are the most common way plants deter predators. Some examples of secondary metabolites are atropine, nicotine, THC and caffeine. Humans have found these secondary metabolite compounds a rich source of materials for medicines.

First peoples herbal treatments revealed these secondary metabolites to the world. For example, Indigenous peoples have long used the bark of willow shrubs and alder trees for a tea, tonic or poultice to reduce inflammation.

You will learn more about the inflammation response by the immune system in chapter Both willow and alder bark contain the compound salicin. Most of us have this compound in our medicine cupboard in the form of salicylic acid or aspirin. Aspirin has been proved to reduce pain and inflammation, and once in our cells salicin converts to salicylic acid.

So how does it work? Salicin or aspirin acts as an enzyme inhibitor. In the inflammatory response two enzymes, COX1 and COX2 are key to this process. Salicin or aspirin specifically modifies an amino acid serine in the active site of these two related enzymes.

This modification of the active sites does not allow the normal substrate to bind and so the inflammatory process is disrupted. As you have read in this chapter, this makes it competitive enzyme inhibitor.

Enzymes are key components of metabolic pathways. Understanding how enzymes work and how they can be regulated are key principles behind the development of many of the pharmaceutical drugs on the market today. Biologists working in this field collaborate with other scientists to design drugs Figure 4.

Consider statins for example—statins is the name given to one class of drugs that can reduce cholesterol levels. These compounds are inhibitors of the enzyme HMG-CoA reductase, which is the enzyme that synthesizes cholesterol from lipids in the body.

By inhibiting this enzyme, the level of cholesterol synthesized in the body can be reduced. Similarly, acetaminophen, popularly marketed under the brand name Tylenol, is an inhibitor of the enzyme cyclooxygenase. While it is used to provide relief from fever and inflammation pain , its mechanism of action is still not completely understood.

How are drugs discovered? One of the biggest challenges in drug discovery is identifying a drug target. A drug target is a molecule that is literally the target of the drug. In the case of statins, HMG-CoA reductase is the drug target. Drug targets are identified through painstaking research in the laboratory.

Identifying the target alone is not enough; scientists also need to know how the target acts inside the cell and which reactions go awry in the case of disease.

Once the target and the pathway are identified, then the actual process of drug design begins. In this stage, chemists and biologists work together to design and synthesize molecules that can block or activate a particular reaction. However, this is only the beginning: If and when a drug prototype is successful in performing its function, then it is subjected to many tests from in vitro experiments to clinical trials before it can get approval from the U.

Food and Drug Administration to be on the market. Many enzymes do not work optimally, or even at all, unless bound to other specific non-protein helper molecules. They may bond either temporarily through ionic or hydrogen bonds, or permanently through stronger covalent bonds. Binding to these molecules promotes optimal shape and function of their respective enzymes.

Two examples of these types of helper molecules are cofactors and coenzymes. Cofactors are inorganic ions such as ions of iron and magnesium.

Coenzymes are organic helper molecules, those with a basic atomic structure made up of carbon and hydrogen. Like enzymes, these molecules participate in reactions without being changed themselves and are ultimately recycled and reused.

Vitamins are the source of coenzymes. Some vitamins are the precursors of coenzymes and others act directly as coenzymes. Vitamin C is a direct coenzyme for multiple enzymes that take part in building the important connective tissue, collagen.

Molecules can regulate enzyme function in many ways. The major question remains, however: What are these molecules and where do they come from? Some are cofactors and coenzymes, as you have learned. What other molecules in the cell provide enzymatic regulation such as allosteric modulation, and competitive and non-competitive inhibition?

Perhaps the most relevant sources of regulatory molecules, with respect to enzymatic cellular metabolism, are the products of the cellular metabolic reactions themselves.

In a most efficient and elegant way, cells have evolved to use the products of their own reactions for feedback inhibition of enzyme activity.

Feedback inhibition involves the use of a reaction product to regulate its own further production Figure 4. The cell responds to an abundance of the products by slowing down production during anabolic or catabolic reactions.

Such reaction products may inhibit the enzymes that catalyzed their production through the mechanisms described above. The production of both amino acids and nucleotides is controlled through feedback inhibition. Additionally, ATP is an allosteric regulator of some of the enzymes involved in the catabolic breakdown of sugar, the process that creates ATP.

In this way, when ATP is in abundant supply, the cell can prevent the production of ATP. On the other hand, ADP serves as a positive allosteric regulator an allosteric activator for some of the same enzymes that are inhibited by ATP.

Thus, when relative levels of ADP are high compared to ATP, the cell is triggered to produce more ATP through sugar catabolism. Cells perform the functions of life through various chemical reactions. Catabolic reactions break down complex chemicals into simpler ones and are associated with energy release.

Anabolic processes build complex molecules out of simpler ones and require energy. In studying energy, the term system refers to the matter and environment involved in energy transfers. Entropy is a measure of the disorder of a system. The physical laws that describe the transfer of energy are the laws of thermodynamics.

The first law states that the total amount of energy in the universe is constant. The second law of thermodynamics states that every energy transfer involves some loss of energy in an unusable form, such as heat energy.

Energy comes in different forms: kinetic, potential, and free. The change in free energy of a reaction can be negative releases energy, exergonic or positive consumes energy, endergonic.

All reactions require an initial input of energy to proceed, called the activation energy. Enzymes are chemical catalysts that speed up chemical reactions by lowering their activation energy. Enzymes have an active site with a unique chemical environment that fits particular chemical reactants for that enzyme, called substrates.

Enzymes and substrates are thought to bind according to an induced-fit model. Enzyme action is regulated to conserve resources and respond optimally to the environment. activation energy: the amount of initial energy necessary for reactions to occur.

allosteric inhibition: the mechanism for inhibiting enzyme action in which a regulatory molecule binds to a second site not the active site and initiates a conformation change in the active site, preventing binding with the substrate. anabolic: describes the pathway that requires a net energy input to synthesize complex molecules from simpler ones.

catabolic: describes the pathway in which complex molecules are broken down into simpler ones, yielding energy as an additional product of the reaction.

endergonic: describes a chemical reaction that results in products that store more chemical potential energy than the reactants. exergonic: describes a chemical reaction that results in products with less chemical potential energy than the reactants, plus the release of free energy.

feedback inhibition: a mechanism of enzyme activity regulation in which the product of a reaction or the final product of a series of sequential reactions inhibits an enzyme for an earlier step in the reaction series.

metabolism: all the chemical reactions that take place inside cells, including those that use energy and those that release energy.

To me, this mess of lines looks like a map of a very large subway system, or possibly a fancy circuit board. In fact, it's a diagram of the core metabolic pathways in a eukaryotic cell, such as the cells that make up the human body.

Each line is a reaction, and each circle is a reactant or product. Abstract diagram representing core eukaryotic metabolic networks. The main point of the diagram is to indicate that metabolism is complex and highly interconnected, with many different pathways that feed into one another.

Image credit: "Metabolism diagram," by Zlir'a public domain. In the metabolic web of the cell, some of the chemical reactions release energy and can happen spontaneously without energy input. However, others need added energy in order to take place. Just as you must continually eat food to replace what your body uses, so cells need a continual inflow of energy to power their energy-requiring chemical reactions.

In fact, the food you eat is the source of the energy used by your cells! To make the idea of metabolism more concrete, let's look at two metabolic processes that are crucial to life on earth: those that build sugars, and those that break them down.

Breaking down glucose: Cellular respiration. During this process, a glucose molecule is broken down gradually, in many small steps. However, the process has an overall reaction of:. Breaking down glucose releases energy, which is captured by the cell in the form of adenosine triphosphate , or ATP.

ATP is a small molecule that gives cells a convenient way to briefly store energy. Once it's made, ATP can be used by other reactions in the cell as an energy source. Building up glucose: Photosynthesis. As an example of an energy-requiring metabolic pathway, let's flip that last example around and see how a sugar molecule is built.

Sugars like glucose are made by plants in a process called photosynthesis. In photosynthesis, plants use the energy of sunlight to convert carbon dioxide gas into sugar molecules.

Photosynthesis takes place in many small steps, but its overall reaction is just the cellular respiration reaction flipped backwards:. Like us, plants need energy to power their cellular processes, so some of the sugars are used by the plant itself. They can also provide a food source for animals that eat the plant, like the squirrel below.

In both cases, the glucose will be broken down through cellular respiration, generating ATP to keep cells running. Left: image of a tree with acorns growing on it.

Right: image of a squirrel eating an acorn. Image credit: OpenStax Biology. Anabolic and catabolic pathways. The processes of making and breaking down glucose molecules are both examples of metabolic pathways. A metabolic pathway is a series of connected chemical reactions that feed one another.

The pathway takes in one or more starting molecules and, through a series of intermediates, converts them into products.

Metabolic pathways can be broadly divided into two categories based on their effects. Photosynthesis, which builds sugars out of smaller molecules, is a "building up," or anabolic , pathway. In contrast, cellular respiration breaks sugar down into smaller molecules and is a "breaking down," or catabolic , pathway.

Anabolic pathway: small molecules are assembled into larger ones. Energy is typically required. Catabolic pathway: large molecules are broken down into small ones.

Energy is typically released. Anabolic pathways build complex molecules from simpler ones and typically need an input of energy. Building glucose from carbon dioxide is one example. Other examples include the synthesis of proteins from amino acids, or of DNA strands from nucleic acid building blocks nucleotides.

These biosynthetic processes are critical to the life of the cell, take place constantly, and use energy carried by ATP and other short-term energy storage molecules. Catabolic pathways involve the breakdown of complex molecules into simpler ones and typically release energy.

Energy stored in the bonds of complex molecules, such as glucose and fats, is released in catabolic pathways. It's then harvested in forms that can power the work of the cell for instance, through the synthesis of ATP.

Instead, each reaction step in a pathway is facilitated, or catalyzed, by a protein called an enzyme. You can learn more about enzymes and how they control biochemical reactions in the enzymes topic.

Want to join the conversation? Log in. Sort by: Top Voted. Manuel Huertas Luna. Posted 8 years ago. I'm curious about how ATP ended up being the energy currency for both plants and animals, why the same molecule? Is because of a common ancestor? Is there any cell that doesn't use ATP as its "energy currency"?

Downvote Button navigates to signup page. Flag Button navigates to signup page. Show preview Show formatting options Post answer.

Matt B. Yes, it is because of the common ancestor. If there was a different, more efficient molecule then this would have been used instead. Keep in mind that in the long run only the most effective processes and molecules can transferred by generations. Posted a year ago. Why is it that ATP happens to resemble an adenine base in DNA?

Are they related in any way beyond structure? Is the adenine base special? Is there another energy currency molecule like ATP? Can we artificially create another energy currency molecule?

Energy is required in order Energy metabolism basics build molecules into larger macromolecules like proteinsbaxics to turn emtabolism into organelles and cells, which then turn into tissues, Energy metabolism basics, basicw organ systems, and Energy metabolism basics into Energy metabolism basics Calcium and liver health. Your body metavolism new macromolecules from the nutrients in food. Energy comes from sunlight, which plants capture and, via photosynthesis, use it to transform carbon dioxide in the air into the molecule glucose. When the glucose bonds are broken, energy is released. Bacteria, plants, and animals including humans harvest the energy in glucose via a biological process called cellular respiration. In this process oxygen is required and the chemical energy of glucose is gradually released in a series of chemical reactions.

Energy metabolism basics -

During this process, a glucose molecule is broken down gradually, in many small steps. However, the process has an overall reaction of:. Breaking down glucose releases energy, which is captured by the cell in the form of adenosine triphosphate , or ATP.

ATP is a small molecule that gives cells a convenient way to briefly store energy. Once it's made, ATP can be used by other reactions in the cell as an energy source. Building up glucose: Photosynthesis. As an example of an energy-requiring metabolic pathway, let's flip that last example around and see how a sugar molecule is built.

Sugars like glucose are made by plants in a process called photosynthesis. In photosynthesis, plants use the energy of sunlight to convert carbon dioxide gas into sugar molecules. Photosynthesis takes place in many small steps, but its overall reaction is just the cellular respiration reaction flipped backwards:.

Like us, plants need energy to power their cellular processes, so some of the sugars are used by the plant itself. They can also provide a food source for animals that eat the plant, like the squirrel below.

In both cases, the glucose will be broken down through cellular respiration, generating ATP to keep cells running. Left: image of a tree with acorns growing on it. Right: image of a squirrel eating an acorn.

Image credit: OpenStax Biology. Anabolic and catabolic pathways. The processes of making and breaking down glucose molecules are both examples of metabolic pathways. A metabolic pathway is a series of connected chemical reactions that feed one another.

The pathway takes in one or more starting molecules and, through a series of intermediates, converts them into products. Metabolic pathways can be broadly divided into two categories based on their effects.

Photosynthesis, which builds sugars out of smaller molecules, is a "building up," or anabolic , pathway. In contrast, cellular respiration breaks sugar down into smaller molecules and is a "breaking down," or catabolic , pathway.

Anabolic pathway: small molecules are assembled into larger ones. Energy is typically required. Catabolic pathway: large molecules are broken down into small ones. Energy is typically released.

Anabolic pathways build complex molecules from simpler ones and typically need an input of energy. Building glucose from carbon dioxide is one example. Other examples include the synthesis of proteins from amino acids, or of DNA strands from nucleic acid building blocks nucleotides.

These biosynthetic processes are critical to the life of the cell, take place constantly, and use energy carried by ATP and other short-term energy storage molecules. Catabolic pathways involve the breakdown of complex molecules into simpler ones and typically release energy. Energy stored in the bonds of complex molecules, such as glucose and fats, is released in catabolic pathways.

It's then harvested in forms that can power the work of the cell for instance, through the synthesis of ATP. Instead, each reaction step in a pathway is facilitated, or catalyzed, by a protein called an enzyme. You can learn more about enzymes and how they control biochemical reactions in the enzymes topic.

Want to join the conversation? Log in. Sort by: Top Voted. Manuel Huertas Luna. Posted 8 years ago. I'm curious about how ATP ended up being the energy currency for both plants and animals, why the same molecule? Is because of a common ancestor? Is there any cell that doesn't use ATP as its "energy currency"?

Downvote Button navigates to signup page. Flag Button navigates to signup page. Show preview Show formatting options Post answer. Matt B. Yes, it is because of the common ancestor.

If there was a different, more efficient molecule then this would have been used instead. Keep in mind that in the long run only the most effective processes and molecules can transferred by generations. Posted a year ago. Why is it that ATP happens to resemble an adenine base in DNA?

Are they related in any way beyond structure? Is the adenine base special? Is there another energy currency molecule like ATP? Can we artificially create another energy currency molecule?

Posted 7 months ago. Both ATP and DNA are nucleic acids. All nucleic acids have 3 parts. A pentose sugar A sugar with 5 carbon molecules 2. Phosphate group s 3. A nitrogen base. DNA and ATP have the same nitrogen base- Adenine, present. ATP is specially called an energy currency because it has an easily breakable bond between 2 of its phosphate groups.

There are several other triphosphate molecules present in cells like GTP and CTP that play various roles, but ATP is the main 'energy trading' molecule. Triphosphate molecules can be synthetically created under the right conditions, our cells will still rely on ATP. Comment Button navigates to signup page.

So basically, Metabolism is the core of a cell. Annual Review of Plant Biology. Journal of Plant Physiology. BMB Reports. Archived PDF from the original on 24 October Retrieved 18 September Current Opinion in Structural Biology.

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Clarendon Press. Nicholls DG, Ferguson SJ Academic Press Inc. Wood HG February Wikiversity has learning resources about Topic:Biochemistry. Wikibooks has more on the topic of: Metabolism.

Look up metabolism in Wiktionary, the free dictionary. Wikimedia Commons has media related to Metabolism. Articles related to Metabolism. Metabolism map. Carbon fixation. Photo- respiration. Pentose phosphate pathway. Citric acid cycle. Glyoxylate cycle.

Urea cycle. Fatty acid synthesis. Fatty acid elongation. Beta oxidation. beta oxidation. Glyco- genolysis. Glyco- genesis. Glyco- lysis. Gluconeo- genesis. Pyruvate decarb- oxylation. Keto- lysis. Keto- genesis. feeders to gluconeo- genesis.

Light reaction. Oxidative phosphorylation. Amino acid deamination. Citrate shuttle. MVA pathway. MEP pathway. Shikimate pathway. Glycosyl- ation. Sugar acids. Simple sugars. Nucleotide sugars. Propionyl -CoA. Acetyl -CoA. Oxalo- acetate. Succinyl -CoA. α-Keto- glutarate.

Ketone bodies. Respiratory chain. Serine group. Branched-chain amino acids. Aspartate group. Amino acids. Ascorbate vitamin C.

Bile pigments. Cobalamins vitamin B Various vitamin Bs. Calciferols vitamin D. Retinoids vitamin A. Nucleic acids. Terpenoid backbones. Bile acids. Glycero- phospholipids. Fatty acids. Glyco- sphingolipids. Polyunsaturated fatty acids.

Endo- cannabinoids. Metabolism , catabolism , anabolism. Metabolic pathway Metabolic network Primary nutritional groups. Purine metabolism Nucleotide salvage Pyrimidine metabolism Purine nucleotide cycle. Pentose phosphate pathway Fructolysis Polyol pathway Galactolysis Leloir pathway. Glycosylation N-linked O-linked.

Photosynthesis Anoxygenic photosynthesis Chemosynthesis Carbon fixation DeLey-Doudoroff pathway Entner-Doudoroff pathway.

Xylose metabolism Radiotrophism. Fatty acid degradation Beta oxidation Fatty acid synthesis. Steroid metabolism Sphingolipid metabolism Eicosanoid metabolism Ketosis Reverse cholesterol transport.

Metal metabolism Iron metabolism Ethanol metabolism Phospagen system ATP-PCr. Fructose-bisphosphate aldolase Aldolase A , B , C Triosephosphate isomerase.

Glyceraldehyde 3-phosphate dehydrogenase Phosphoglycerate kinase Phosphoglycerate mutase Enolase Pyruvate kinase PKLR , PKM2. Pyruvate carboxylase Phosphoenolpyruvate carboxykinase. Lactate dehydrogenase. Alanine transaminase. Glycerol kinase Glycerol dehydrogenase.

Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase PFKFB1 , PFKFB2 , PFKFB3 , PFKFB4 Bisphosphoglycerate mutase. Metabolism : carbohydrate metabolism fructose and galactose enzymes. Hepatic fructokinase Aldolase B Triokinase.

Sorbitol dehydrogenase Aldose reductase. Lactose synthase Lactase. Mannose phosphate isomerase. Metabolism : carbohydrate metabolism proteoglycan enzymes. L-xylulose reductase L-gulonolactone oxidase UDP-glucuronate 5'-epimerase Xylosyltransferase Sulfotransferase Heparan sulfate EXT1 EXT2 Chondroitin sulfate PAPSS1 PAPSS2.

Iduronatesulfatase Iduronidase. Heparan sulfamidase N-acetyltransferase Alpha-N-acetylglucosaminidase Glucuronidase N-acetylglucosaminesulfatase.

Arylsulfatase B Galactosamine-6 sulfatase Beta-galactosidase GLB1. Metabolism : carbohydrate metabolism · glycoprotein enzymes.

Dolichol kinase GCS1 Oligosaccharyltransferase. Neuraminidase Beta-galactosidase Hexosaminidase mannosidase alpha-Mannosidase beta-mannosidase Aspartylglucosaminidase Fucosidase NAGA.

N-acetylglucosaminephosphate transferase. Metabolism , lipid metabolism , glycolipid enzymes. Glycosyltransferase Sulfotransferase. From ganglioside Beta-galactosidase Hexosaminidase A Neuraminidase Glucocerebrosidase From globoside Hexosaminidase B Alpha-galactosidase Beta-galactosidase Glucocerebrosidase From sphingomyelin Sphingomyelin phosphodiesterase Sphingomyelin phosphodiesterase 1 From sulfatide Arylsulfatase A Galactosylceramidase.

Ceramidase ACER1 ACER2 ACER3 ASAH1 ASAH2 ASAH2B ASAH2C. Sphingosine kinase. Palmitoyl protein thioesterase Tripeptidyl peptidase I CLN3 CLN5 CLN6 CLN8.

Serine C-palmitoyltransferase SPTLC1 Ceramide glucosyltransferase UGCG. Metabolism : lipid metabolism — eicosanoid metabolism enzymes. Phospholipase A2 Phospholipase C Diacylglycerol lipase. Cyclooxygenase PTGS1 PTGS2 PGD2 synthase PGE synthase Prostaglandin-E2 9-reductase PGI2 synthase TXA synthase.

ATP citrate lyase Acetyl-CoA carboxylase. Beta-ketoacyl-ACP synthase Β-Ketoacyl ACP reductase 3-Hydroxyacyl ACP dehydrase Enoyl ACP reductase.

Stearoyl-CoA desaturase Glycerolphosphate dehydrogenase Thiokinase. Carnitine palmitoyltransferase I Carnitine-acylcarnitine translocase Carnitine palmitoyltransferase II.

Acyl CoA dehydrogenase ACADL ACADM ACADS ACADVL ACADSB Enoyl-CoA hydratase MTP : HADH HADHA HADHB Acetyl-CoA C-acyltransferase. Enoyl CoA isomerase 2,4 Dienoyl-CoA reductase. Propionyl-CoA carboxylase. Hydroxyacyl-Coenzyme A dehydrogenase. Malonyl-CoA decarboxylase.

Long-chain-aldehyde dehydrogenase. Metabolism : amino acid metabolism - urea cycle enzymes. Carbamoyl phosphate synthetase I Ornithine transcarbamylase. Argininosuccinate synthetase Argininosuccinate lyase Arginase.

N-Acetylglutamate synthase Ornithine translocase. Enzymes involved in neurotransmission. Histidine decarboxylase. Histamine N-methyltransferase Diamine oxidase.

Tyrosine hydroxylase Aromatic L-amino acid decarboxylase Dopamine beta-hydroxylase Phenylethanolamine N-methyltransferase. Catechol-O-methyl transferase Monoamine oxidase A B.

Glutamate decarboxylase. Tryptophan hydroxylase Aromatic L-amino acid decarboxylase Aralkylamine N-acetyltransferase Acetylserotonin O-methyltransferase.

Nitric oxide synthase NOS1 , NOS2 , NOS3. Choline acetyltransferase. Cholinesterase Acetylcholinesterase , Butyrylcholinesterase. Enzymes involved in the metabolism of heme and porphyrin.

Aminolevulinic acid synthase ALAS1 ALAS2. Porphobilinogen synthase Porphobilinogen deaminase Uroporphyrinogen III synthase Uroporphyrinogen III decarboxylase. Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Ferrochelatase.

Heme oxygenase Biliverdin reductase. glucuronosyltransferase UGT1A1. Metabolism of vitamins , coenzymes, and cofactors. Retinol binding protein. Alpha-tocopherol transfer protein.

liver Sterol hydroxylase or CYP27A1 renal Hydroxyvitamin D 3 1-alpha-hydroxylase or CYP27B1 degradation 1,Dihydroxyvitamin D 3 hydroxylase or CYP24A1. Vitamin K epoxide reductase. Thiamine diphosphokinase.

Indoleamine 2,3-dioxygenase Formamidase. Pantothenate kinase. Dihydropteroate synthase Dihydrofolate reductase Serine hydroxymethyltransferase. Methylenetetrahydrofolate reductase. MMAA MMAB MMACHC MMADHC. L-gulonolactone oxidase. Riboflavin kinase.

GTP cyclohydrolase I 6-pyruvoyltetrahydropterin synthase Sepiapterin reductase. PCBD1 PTS QDPR. MOCS1 MOCS2 MOCS3 Gephyrin.

Metabolism : Protein metabolism , synthesis and catabolism enzymes. Essential amino acids are in Capitals. Saccharopine dehydrogenase Glutaryl-CoA dehydrogenase.

D-cysteine desulfhydrase. L-threonine dehydrogenase. Histidine ammonia-lyase Urocanate hydratase Formiminotransferase cyclodeaminase. Ornithine aminotransferase Ornithine decarboxylase Agmatinase. Glutamate dehydrogenase. Branched-chain amino acid aminotransferase Branched-chain alpha-keto acid dehydrogenase complex Enoyl-CoA hydratase 3-hydroxyisobutyryl-CoA hydrolase 3-hydroxyisobutyrate dehydrogenase Methylmalonate semialdehyde dehydrogenase.

Branched-chain amino acid aminotransferase Branched-chain alpha-keto acid dehydrogenase complex 3-hydroxymethylbutyryl-CoA dehydrogenase. Threonine aldolase.

Propionyl-CoA carboxylase Methylmalonyl CoA epimerase Methylmalonyl-CoA mutase. Metabolism : amino acid metabolism nucleotide enzymes. Ribose-phosphate diphosphokinase Amidophosphoribosyltransferase Phosphoribosylglycinamide formyltransferase AIR synthetase FGAM cyclase Phosphoribosylaminoimidazole carboxylase Phosphoribosylaminoimidazolesuccinocarboxamide synthase IMP synthase.

Adenylosuccinate synthase Adenylosuccinate lyase reverse AMP deaminase. IMP dehydrogenase GMP synthase reverse GMP reductase.

Hypoxanthine-guanine phosphoribosyltransferase Adenine phosphoribosyltransferase. Adenosine deaminase Purine nucleoside phosphorylase Guanine deaminase Xanthine oxidase Urate oxidase.

CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase. CTP synthetase. Ribonucleotide reductase Nucleoside-diphosphate kinase DCMP deaminase Thymidylate synthase Dihydrofolate reductase.

Acetyl-Coenzyme A acetyltransferase HMG-CoA synthase regulated step. HMG-CoA lyase 3-hydroxybutyrate dehydrogenase Thiophorase.

HMG-CoA reductase. Mevalonate kinase Phosphomevalonate kinase Pyrophosphomevalonate decarboxylase Isopentenyl-diphosphate delta isomerase. Dimethylallyltranstransferase Geranyl pyrophosphate.

Farnesyl-diphosphate farnesyltransferase Squalene monooxygenase Lanosterol synthase. Lanosterol 14α-demethylase Sterol-C5-desaturase-like 7-Dehydrocholesterol reductase. Cholesterol 7α-hydroxylase Sterol hydroxylase. Cholesterol side-chain cleavage. Aromatase 17β- HSD. Steroid metabolism : sulfatase Steroid sulfatase sulfotransferase SULT1A1 SULT2A1 Steroidogenic acute regulatory protein Cholesterol total synthesis Reverse cholesterol transport.

Metabolism : carbohydrate metabolism · pentose phosphate pathway enzymes. Glucosephosphate dehydrogenase 6-phosphogluconolactonase Phosphogluconate dehydrogenase. Phosphopentose isomerase Phosphopentose epimerase Transketolase Transaldolase. Metabolism - non-mevalonate pathway enzymes.

DXP synthase DXP reductoisomerase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase 4- cytidine 5'-diphospho C-methyl-D-erythritol kinase 4-hydroxymethylbutenyl diphosphate synthase 4-hydroxymethylbutenyl diphosphate reductase.

Food science. Allergy Engineering Microbiology Nutrition Diet clinical Processing Processing aids Psychology Quality Sensory analysis Discrimination testing Rheology Storage Technology. Food chemistry. Additives Carbohydrates Coloring Enzymes Essential fatty acids Flavors Fortification Lipids "Minerals" Chemical elements Proteins Vitamins Water.

Food preservation. Biopreservation Canning Cold chain Curing Drying Fermentation Freeze-drying Freezing Hurdle technology Irradiation Jamming Jellying Jugging Modified atmosphere Pascalization Pickling Potting Confit Potjevleesch Salting Smoking Sugaring Tyndallization Vacuum packing.

Food portal Category: Food preservation. Manufacturing Packaging Marketing Foodservice Fortification. Consumer food safety. Flavorings Monosodium glutamate MSG Salt Sugar High-fructose corn syrup. Amoebiasis Anisakiasis Cryptosporidiosis Cyclosporiasis Diphyllobothriasis Enterobiasis Fasciolopsiasis Fasciolosis Giardiasis Gnathostomiasis Paragonimiasis Toxocariasis Toxoplasmosis Trichinosis Trichuriasis.

Botulism Campylobacter jejuni Clostridium perfringens Cronobacter Enterovirus Escherichia coli OH4 Escherichia coli OH7 Hepatitis A Hepatitis E Listeria Norovirus Rotavirus Salmonella Vibrio cholerae.

Chlorpyrifos DDT Lindane Malathion Methamidophos. Benzoic acid Ethylenediaminetetraacetic acid EDTA Sodium benzoate. Acesulfame potassium Aspartame controversy Saccharin Sodium cyclamate Sorbitol Sucralose.

Aflatoxin Arsenic contamination of groundwater Benzene in soft drinks Bisphenol A Dieldrin Diethylstilbestrol Dioxin Mycotoxins Nonylphenol Shellfish poisoning. Devon colic Swill milk scandal Esing Bakery incident Bradford sweets poisoning English beer poisoning Morinaga Milk arsenic poisoning incident Minamata disease Iraq poison grain disaster Toxic oil syndrome Austrian diethylene glycol wine scandal United Kingdom BSE outbreak Australian meat substitution scandal Jack in the Box E.

coli outbreak Odwalla E. coli outbreak North American E. coli outbreaks ICA meat repackaging controversy Canada listeriosis outbreak Chinese milk scandal Irish pork crisis United States salmonellosis outbreak Germany E. coli outbreak United States listeriosis outbreak Bihar school meal poisoning incident horse meat scandal Mozambique funeral beer poisoning Brazil Operation Weak Meat — South African listeriosis outbreak Australian rockmelon listeriosis outbreak Australian strawberry contamination Food safety incidents in China Food safety incidents in Taiwan Foodborne illness outbreaks death toll United States.

Acceptable daily intake E number Food labeling regulations Food libel laws Food safety in Australia International Food Safety Network ISO Nutrition facts label Organic certification Quality Assurance International United Kingdom food information regulations.

Centre for Food Safety Hong Kong European Food Safety Authority Food and Drug Administration Food Information and Control Agency Spain Food Standards Agency United Kingdom Institute for Food Safety and Health International Food Safety Network Ministry of Food and Drug Safety South Korea Spanish Agency for Food Safety and Nutrition.

Curing food preservation Food and drink prohibitions Food marketing Food politics Food preservation Food quality Genetically modified food Conspiracy theories.

Food portal Drink portal Category Commons Cookbook WikiProject. Acid-hydrolyzed vegetable protein. Acesulfame potassium Alitame Aspartame Aspartame-acesulfame salt Dulcin Glucin Hydrogenated starch hydrolysates Neohesperidin dihydrochalcone Neotame NutraSweet Nutrinova Saccharin Sodium cyclamate Sucralose.

Cheese analogues Coffee substitutes Egg substitutes Meat analogues bacon list Milk substitutes Phyllodulcin Salt substitutes. Food safety List of food additives. Food power Food security Famine Malnutrition Overnutrition.

International Association for Food Protection Food and Drug Administration Food and Agriculture Organization National Agriculture and Food Research Organization National Food and Drug Authority.

Authority control databases. France BnF data Germany Israel United States Latvia Czech Republic. Encyclopedia of Modern Ukraine. Categories : Metabolism Underwater diving physiology. Hidden categories: CS1 errors: periodical ignored CS1 maint: DOI inactive as of January Webarchive template wayback links Articles with short description Short description is different from Wikidata Use dmy dates from August Articles with excerpts Articles containing Greek-language text All articles with unsourced statements Articles with unsourced statements from December Articles with unsourced statements from June Pages displaying wikidata descriptions as a fallback via Module:Annotated link Commons category link from Wikidata Featured articles Articles with BNF identifiers Articles with BNFdata identifiers Articles with GND identifiers Articles with J9U identifiers Articles with LCCN identifiers Articles with LNB identifiers Articles with NKC identifiers Articles with EMU identifiers.

Toggle limited content width. Chemistry of life. Key components Biomolecules Enzymes Gene expression Metabolism. List of biochemists Biochemist List of biochemists. Biomolecule families Carbohydrates : Alcohols Glycoproteins Glycosides Lipids : Eicosanoids Fatty acids Fatty-acid metabolism Glycerides Phospholipids Sphingolipids Cholesterol Steroids Nucleic acids : Nucleobases Nucleosides Nucleotides Nucleotide metabolism Proteins : Amino acids Amino acid metabolism Other: Tetrapyrroles Heme.

Chemical synthesis Artificial gene synthesis Biomimetic synthesis Bioretrosynthesis Biosynthesis Chemosynthesis Convergent synthesis Custom peptide synthesis Direct process Divergent synthesis Electrosynthesis Enantioselective synthesis Fully automated synthesis Hydrothermal synthesis LASiS Mechanosynthesis One-pot synthesis Organic synthesis Peptide synthesis Radiosynthesis Retrosynthesis Semisynthesis Solid-phase synthesis Solvothermal synthesis Total synthesis Volume combustion synthesis.

Biochemistry fields Molecular biology Cell biology Chemical biology Bioorthogonal chemistry Medicinal chemistry Pharmacology Clinical chemistry Neurochemistry Bioorganic chemistry Bioorganometallic chemistry Bioinorganic chemistry Biophysical chemistry Bacteriology parasitology virology immunology.

Glossaries Glossary of biology Glossary of chemistry. Fibrous proteins and globular proteins. Starch , glycogen and cellulose. organic compound. Library resources about Metabolism. Online books Resources in your library Resources in other libraries.

Electron acceptors other than oxygen. Fatty acid metabolism Fatty acid degradation Beta oxidation Fatty acid synthesis. to oxaloacetate : Pyruvate carboxylase Phosphoenolpyruvate carboxykinase. Hunter , Hurler Iduronatesulfatase Iduronidase.

To glycosphingolipid Glycosyltransferase Sulfotransferase. Malonyl-CoA synthesis ATP citrate lyase Acetyl-CoA carboxylase. Acyl transport Carnitine palmitoyltransferase I Carnitine-acylcarnitine translocase Carnitine palmitoyltransferase II. General Acyl CoA dehydrogenase ACADL ACADM ACADS ACADVL ACADSB Enoyl-CoA hydratase MTP : HADH HADHA HADHB Acetyl-CoA C-acyltransferase.

mitochondrial matrix : Carbamoyl phosphate synthetase I Ornithine transcarbamylase. anabolism: Tyrosine hydroxylase Aromatic L-amino acid decarboxylase Dopamine beta-hydroxylase Phenylethanolamine N-methyltransferase.

anabolism: Glutamate decarboxylase. anabolism: Choline acetyltransferase. early mitochondrial: Aminolevulinic acid synthase ALAS1 ALAS2. spleen: Heme oxygenase Biliverdin reductase. Vitamin A Retinol binding protein. Thiamine B 1 Thiamine diphosphokinase.

Tetrahydrobiopterin GTP cyclohydrolase I 6-pyruvoyltetrahydropterin synthase Sepiapterin reductase. see below. Anabolism CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase.

To HMG-CoA Acetyl-Coenzyme A acetyltransferase HMG-CoA synthase regulated step. To lanosterol Farnesyl-diphosphate farnesyltransferase Squalene monooxygenase Lanosterol synthase.

To pregnenolone Cholesterol side-chain cleavage. To androgens 17α-Hydroxylase 17,Lyase 3β- HSD 17β- HSD 5α-Reductase 1 2. Allergy Engineering Microbiology Nutrition Diet clinical Processing Processing aids Psychology Quality Sensory analysis Discrimination testing Rheology Storage Technology v t e Food chemistry Additives Carbohydrates Coloring Enzymes Essential fatty acids Flavors Fortification Lipids "Minerals" Chemical elements Proteins Vitamins Water.

v t e Food preservation Biopreservation Canning Cold chain Curing Drying Fermentation Freeze-drying Freezing Hurdle technology Irradiation Jamming Jellying Jugging Modified atmosphere Pascalization Pickling Potting Confit Potjevleesch Salting Smoking Sugaring Tyndallization Vacuum packing.

Manufacturing Packaging Marketing Foodservice Fortification v t e Consumer food safety Adulterants , food contaminants 3-MCPD Aldicarb Antibiotic use in livestock Cyanide Formaldehyde HGH controversies Lead poisoning Melamine Mercury in fish Sudan I.

v t e Artificial foods Artificial fat substitutes Olestra.

Metabolism pronounced: meh-TAB-uh-liz-um is Energy metabolism basics Enerfy Energy metabolism basics metabooism the body's Polyphenols and cognitive decline prevention that change food metabolims energy. Our bodies need this Energy metabolism basics to do everything from moving to thinking to emtabolism. Specific proteins in the body control the chemical reactions of metabolism. Thousands of metabolic reactions happen at the same time — all regulated by the body — to keep our cells healthy and working. After we eat food, the digestive system uses enzymes to:. The body can use sugar, amino acids, and fatty acids as energy sources when needed. Financial aid available. Energy metabolism basics insight into a topic and metabllism the fundamentals. Instructor: Seyun Vasics. Included with Coursera Plus. Add this credential to your LinkedIn profile, resume, or CV. Share it on social media and in your performance review. Everyone knows that energy is essential for sustaining life. Energy metabolism basics

Author: Samukora

4 thoughts on “Energy metabolism basics

  1. Im Vertrauen gesagt ist meiner Meinung danach offenbar. Ich wollte dieses Thema nicht entwickeln.

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