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Many enzymes don’t work optimally, or even at all, unless bound to other specific non-protein helper molecules, either temporarily through ionic or hydrogen bonds or permanently through stronger covalent bonds. Two types of helper molecules are cofactors and coenzymes . Binding to these molecules promotes optimal conformation and function for their respective enzymes. Cofactors are inorganic ions such as iron (Fe++) and magnesium (Mg++). One example of an enzyme that requires a metal ion as a cofactor is the enzyme that builds DNA molecules, DNA polymerase, which requires bound zinc ion (Zn++) to function. Coenzymes are organic helper molecules, with a basic atomic structure made up of carbon and hydrogen, which are required for enzyme action. The most common sources of coenzymes are dietary vitamins ( [link] ). Some vitamins are precursors to coenzymes and others act directly as coenzymes. Vitamin C is a coenzyme for multiple enzymes that take part in building the important connective tissue component, collagen. An important step in the breakdown of glucose to yield energy is catalysis by a multi-enzyme complex called pyruvate dehydrogenase. Pyruvate dehydrogenase is a complex of several enzymes that actually requires one cofactor (a magnesium ion) and five different organic coenzymes to catalyze its specific chemical reaction. Therefore, enzyme function is, in part, regulated by an abundance of various cofactors and coenzymes, which are supplied primarily by the diets of most organisms.

Shown are the molecular structures for Vitamin A, folic acid, Vitamin B1, Vitamin C, Vitamin B2, Vitamin D2, Vitamin B6, and Vitamin E.
Vitamins are important coenzymes or precursors of coenzymes, and are required for enzymes to function properly. Multivitamin capsules usually contain mixtures of all the vitamins at different percentages.

Enzyme compartmentalization

In eukaryotic cells, molecules such as enzymes are usually compartmentalized into different organelles. This allows for yet another level of regulation of enzyme activity. Enzymes required only for certain cellular processes can be housed separately along with their substrates, allowing for more efficient chemical reactions. Examples of this sort of enzyme regulation based on location and proximity include the enzymes involved in the latter stages of cellular respiration, which take place exclusively in the mitochondria, and the enzymes involved in the digestion of cellular debris and foreign materials, located within lysosomes.

Feedback inhibition in metabolic pathways

Molecules can regulate enzyme function in many ways. A major question remains, however: What are these molecules and where do they come from? Some are cofactors and coenzymes, ions, and organic molecules, as you’ve learned. What other molecules in the cell provide enzymatic regulation, such as allosteric modulation, and competitive and noncompetitive inhibition? The answer is that a wide variety of molecules can perform these roles. Some of these molecules include pharmaceutical and non-pharmaceutical drugs, toxins, and poisons from the environment. Perhaps the most relevant sources of enzyme regulatory molecules, with respect to 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 ( [link] ). The cell responds to the abundance of specific 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.

This diagram shows a metabolic pathway in which three enzymes convert a substrate, in three steps, into a final product. The final product inhibits the first enzyme in the pathway.
Metabolic pathways are a series of reactions catalyzed by multiple enzymes. Feedback inhibition, where the end product of the pathway inhibits an upstream step, is an important regulatory mechanism in cells.

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 produces ATP. In this way, when ATP is abundant, the cell can prevent its further production. Remember that ATP is an unstable molecule that can spontaneously dissociate into ADP. If too much ATP were present in a cell, much of it would go to waste. 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 the catabolism of sugar.

Section summary

Enzymes are chemical catalysts that accelerate chemical reactions at physiological temperatures by lowering their activation energy. Enzymes are usually proteins consisting of one or more polypeptide chains. Enzymes have an active site that provides a unique chemical environment, made up of certain amino acid R groups (residues). This unique environment is perfectly suited to convert particular chemical reactants for that enzyme, called substrates, into unstable intermediates called transition states. Enzymes and substrates are thought to bind with an induced fit, which means that enzymes undergo slight conformational adjustments upon substrate contact, leading to full, optimal binding. Enzymes bind to substrates and catalyze reactions in four different ways: bringing substrates together in an optimal orientation, compromising the bond structures of substrates so that bonds can be more easily broken, providing optimal environmental conditions for a reaction to occur, or participating directly in their chemical reaction by forming transient covalent bonds with the substrates.

Enzyme action must be regulated so that in a given cell at a given time, the desired reactions are being catalyzed and the undesired reactions are not. Enzymes are regulated by cellular conditions, such as temperature and pH. They are also regulated through their location within a cell, sometimes being compartmentalized so that they can only catalyze reactions under certain circumstances. Inhibition and activation of enzymes via other molecules are other important ways that enzymes are regulated. Inhibitors can act competitively, noncompetitively, or allosterically; noncompetitive inhibitors are usually allosteric. Activators can also enhance the function of enzymes allosterically. The most common method by which cells regulate the enzymes in metabolic pathways is through feedback inhibition. During feedback inhibition, the products of a metabolic pathway serve as inhibitors (usually allosteric) of one or more of the enzymes (usually the first committed enzyme of the pathway) involved in the pathway that produces them.

Questions & Answers

Discuss the differences between taste and flavor, including how other sensory inputs contribute to our  perception of flavor.
John Reply
taste refers to your understanding of the flavor . while flavor one The other hand is refers to sort of just a blend things.
Faith
While taste primarily relies on our taste buds, flavor involves a complex interplay between taste and aroma
Kamara
which drugs can we use for ulcers
Ummi Reply
omeprazole
Kamara
what
Renee
what is this
Renee
is a drug
Kamara
of anti-ulcer
Kamara
Omeprazole Cimetidine / Tagament For the complicated once ulcer - kit
Patrick
what is the function of lymphatic system
Nency Reply
Not really sure
Eli
to drain extracellular fluid all over the body.
asegid
The lymphatic system plays several crucial roles in the human body, functioning as a key component of the immune system and contributing to the maintenance of fluid balance. Its main functions include: 1. Immune Response: The lymphatic system produces and transports lymphocytes, which are a type of
asegid
to transport fluids fats proteins and lymphocytes to the blood stream as lymph
Adama
what is anatomy
Oyindarmola Reply
Anatomy is the identification and description of the structures of living things
Kamara
what's the difference between anatomy and physiology
Oyerinde Reply
Anatomy is the study of the structure of the body, while physiology is the study of the function of the body. Anatomy looks at the body's organs and systems, while physiology looks at how those organs and systems work together to keep the body functioning.
AI-Robot
what is enzymes all about?
Mohammed Reply
Enzymes are proteins that help speed up chemical reactions in our bodies. Enzymes are essential for digestion, liver function and much more. Too much or too little of a certain enzyme can cause health problems
Kamara
yes
Prince
how does the stomach protect itself from the damaging effects of HCl
Wulku Reply
little girl okay how does the stomach protect itself from the damaging effect of HCL
Wulku
it is because of the enzyme that the stomach produce that help the stomach from the damaging effect of HCL
Kamara
function of digestive system
Ali Reply
function of digestive
Ali
the diagram of the lungs
Adaeze Reply
what is the normal body temperature
Diya Reply
37 degrees selcius
Xolo
37°c
Stephanie
please why 37 degree selcius normal temperature
Mark
36.5
Simon
37°c
Iyogho
the normal temperature is 37°c or 98.6 °Fahrenheit is important for maintaining the homeostasis in the body the body regular this temperature through the process called thermoregulation which involves brain skin muscle and other organ working together to maintain stable internal temperature
Stephanie
37A c
Wulku
what is anaemia
Diya Reply
anaemia is the decrease in RBC count hemoglobin count and PVC count
Eniola
what is the pH of the vagina
Diya Reply
how does Lysin attack pathogens
Diya
acid
Mary
I information on anatomy position and digestive system and there enzyme
Elisha Reply
anatomy of the female external genitalia
Muhammad Reply
Organ Systems Of The Human Body (Continued) Organ Systems Of The Human Body (Continued)
Theophilus Reply
what's lochia albra
Kizito
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Source:  OpenStax, Biology. OpenStax CNX. Feb 29, 2016 Download for free at http://cnx.org/content/col11448/1.10
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