Enzyme kinetics is a fundamental discipline within biochemistry that seeks to understand the behavior and properties of enzymes. Enzymes are biological catalysts that accelerate chemical reactions by lowering the activation energy required for these processes. By studying enzyme kinetics, researchers can gain insights into the mechanisms by which enzymes catalyze reactions in living organisms.
One example of the importance of understanding enzyme kinetics lies in drug development. Consider a hypothetical case study involving a new potential drug candidate targeting an important enzyme involved in cancer cell growth. Before this drug can be used effectively, it is crucial to determine its efficacy and safety profile. This requires a comprehensive understanding of how the drug interacts with the target enzyme, as well as knowledge about its kinetic parameters such as substrate affinity (Km) and maximum reaction rate (Vmax). Such information can help optimize dosages and predict potential side effects, ultimately contributing to more effective therapies.
The classification of enzymes is an essential aspect of enzyme kinetics research. Enzymes are grouped based on their functional characteristics, such as the type of reaction they catalyze or their mechanism of action. Understanding these classifications enables scientists to better comprehend enzymatic function and identify novel applications in various fields, including medicine, industry, and environmental science. In this article In this article, we will explore the different classifications of enzymes and their significance in understanding enzyme kinetics.
Enzyme Inhibitors: Types and Mechanisms
Imagine a scenario where a patient, suffering from an autoimmune disease, receives a prescription for a medication that promises to alleviate their symptoms. However, upon taking the medication, they experience no improvement in their condition. This lack of response could be attributed to the presence of enzyme inhibitors within the medication.
Enzyme inhibitors are substances that interfere with the normal functioning of enzymes, which play vital roles in biochemical reactions within living organisms. These inhibitors can act by binding reversibly or irreversibly to the active site of an enzyme or by altering its structure through non-competitive inhibition. Reversible inhibitors bind temporarily to the active site, preventing substrate molecules from accessing it. On the other hand, irreversible inhibitors form covalent bonds with amino acid residues at the active site, rendering it permanently inactive.
To better understand the diverse mechanisms employed by enzyme inhibitors, let us delve into some common types:
- Competitive Inhibition: This type occurs when an inhibitor molecule closely resembles the natural substrate and competes for binding at the active site. As a result, this hinders enzymatic activity until either more substrate molecules become available or the concentration of inhibitor decreases.
- Non-competitive Inhibition: Unlike competitive inhibition, non-competitive inhibitors bind to allosteric sites on enzymes rather than competing directly with substrates for active site occupancy. By doing so, these inhibitors alter the conformation of enzymes and inhibit their catalytic function.
- Uncompetitive Inhibition: Here, an inhibitor binds only after substrates have bound to enzymes’ active sites. The formation of this complex prevents product release and reduces overall reaction rates.
- Mixed Inhibition: A mixed inhibitor can bind both free enzyme molecules and those already bound by substrates but exhibits different affinities for each state. Depending on whether it has higher affinity towards unbound or bound states determines if it acts as a competitive or non-competitive inhibitor.
These various types of enzyme inhibition can have profound effects on the regulation of biochemical processes within living organisms. The presence of inhibitors in medications, like the hypothetical scenario mentioned earlier, may hinder enzymatic reactions necessary for therapeutic efficacy.
Transitioning into the subsequent section about “Enzyme Activators: Modes of Action,” we now shift our focus to molecules that enhance enzymatic activity rather than inhibit it. By understanding both inhibition and activation mechanisms, researchers can gain insights into developing improved medical treatments and therapies without inadvertently impeding vital biological functions.
Enzyme Activators: Modes of Action
Enzyme Kinetics: Classification of Enzymes
In the previous section, we explored the diverse mechanisms by which enzyme inhibitors exert their effects. Now, let us delve into the Classification of Enzymes based on their kinetics and how this classification helps us understand their behavior in biochemical reactions.
To illustrate this concept, consider an example involving two hypothetical enzymes, A and B. Both enzymes catalyze the same reaction but exhibit different kinetic properties. Enzyme A follows a Michaelis-Menten kinetic model with typical saturation behavior, while enzyme B demonstrates cooperative kinetics characterized by sigmoidal substrate binding curves.
Understanding the various types of enzymatic behaviors allows researchers to predict and interpret experimental findings accurately. Here are some key classifications of enzymes:
- Simple Enzymes: These enzymes display classical Michaelis-Menten kinetics where they bind substrates independently without cooperativity or allosteric regulation.
- Allosteric Enzymes: In contrast to simple enzymes, these enzymes undergo conformational changes upon binding a regulatory molecule at a site distinct from the active site, resulting in altered activity levels.
- Cooperative Enzymes: These enzymes exhibit positive cooperativity, indicating that substrate binding enhances subsequent substrate affinity.
- Zymogens: Also known as proenzymes or inactive precursors, zymogens require activation through proteolytic cleavage to become fully functional enzymes.
Now let’s evoke an emotional response using bullet points:
- Discovering new enzyme classes expands our understanding of biological processes and provides potential targets for therapeutic intervention.
- The intricate regulation of enzyme activities highlights nature’s remarkable ability to fine-tune cellular functions.
- Unraveling novel enzymatic behaviors contributes to advances in fields like drug discovery and metabolic engineering.
- Studying enzymatic dysregulation can shed light on disease mechanisms and pave the way for innovative treatment strategies.
Additionally, here is a table summarizing common enzyme classifications:
| Classification | Description |
|---|---|
| Simple Enzymes | Follow the classical Michaelis-Menten kinetics, binding substrates independently |
| Allosteric Enzymes | Undergo conformational changes upon binding a regulatory molecule at a distinct site |
| Cooperative Enzymes | Exhibit positive cooperativity, where substrate binding enhances subsequent substrate affinity |
| Zymogens | Inactive precursors that require proteolytic cleavage for activation |
In summary, understanding the classification of enzymes based on their kinetic properties allows us to decipher their behavior in biochemical reactions. This knowledge not only aids in interpreting experimental results but also has broader implications in areas such as drug development and disease research.
Transitioning into the next section about “Different Approaches to Modeling Enzyme Kinetics,” we can explore various computational methods used to analyze enzyme behaviors and predict their kinetics.
Different Approaches to Modeling Enzyme Kinetics
Enzyme Kinetics: Classification of Enzymes
Enzyme Activators: Modes of Action
In the previous section, we explored the various modes of action for enzyme activators. Now, let us delve into another crucial aspect of enzymology – the classification of enzymes based on their kinetics. To illustrate this concept, consider an example where a researcher is studying the activity of several enzymes involved in carbohydrate metabolism.
Classification Based on Reaction Mechanism:
Enzymes can be classified based on their reaction mechanisms and how they interact with substrates. This classification helps to understand the catalytic properties and specificities of different enzymes. Here are four major categories:
- Oxidoreductases: These enzymes facilitate oxidation-reduction reactions by transferring electrons between molecules.
- Transferases: They transfer functional groups from one molecule to another, playing essential roles in processes like amino acid biosynthesis.
- Hydrolases: As the name suggests, hydrolases break chemical bonds through hydrolysis reactions, adding water molecules in the process.
- Lyases: Lyases cleave or form bonds without using water as a reactant, often resulting in structural rearrangements.
Table 1 below summarizes these classifications along with examples of representative enzymes.
| Classification | Example Enzymes |
|---|---|
| Oxidoreductases | Lactate dehydrogenase Alcohol dehydrogenase |
| Transferases | Hexokinase DNA methyltransferase |
| Hydrolases | Amylase Lipase |
| Lyases | Pyruvate decarboxylase Carbonic anhydrase |
Emotional Bullets:
To appreciate the diversity and importance of enzyme classification, consider the following emotional points:
- The intricate network formed by different types of enzymes ensures efficient energy conversion and regulation within living organisms.
- Understanding enzyme classification allows researchers to identify potential drug targets for diseases caused by enzyme dysfunctions, giving hope for the development of effective treatments.
- The complexity of enzymatic reactions highlights the marvels of nature’s design, providing inspiration for scientists seeking solutions to technological challenges.
- Enzyme classification underscores the interdependence between different biological processes, emphasizing the delicate balance required for life.
Methods for Measuring Enzyme Kinetics:
By employing these techniques, scientists can gain insights into key parameters such as reaction rates and substrate affinities. Let us now delve into these methodologies without delay.
Methods for Measuring Enzyme Kinetics
Enzyme Kinetics: Classification of Enzymes
Different Approaches to Modeling Enzyme Kinetics have provided valuable insights into the complex nature of enzyme reactions. Now, let us delve further into the classification of enzymes based on their kinetic properties. To illustrate this concept, consider the hypothetical example of two enzymes, A and B.
Enzyme A exhibits Michaelis-Menten kinetics, where the rate of reaction depends on the concentration of substrate. As the substrate concentration increases, so does the rate until it reaches a maximum value known as Vmax. On the other hand, enzyme B follows allosteric kinetics, displaying sigmoidal curves in response to changes in substrate concentration. This behavior suggests that enzyme B has multiple binding sites for its substrates and undergoes conformational changes upon binding.
To better understand the different types of enzymes encountered in biochemical systems, we can classify them based on various criteria:
- Substrate specificity: Some enzymes are highly specific and only catalyze one particular reaction with a specific substrate. These are termed monospecific enzymes. Others exhibit promiscuity and can act upon multiple substrates or even catalyze more than one type of reaction.
- Regulatory mechanisms: Certain enzymes undergo regulation through inhibitory molecules or activators to modulate their activity levels. This allows cells to regulate metabolic pathways dynamically.
- Catalytic mechanism: Enzymes may employ different strategies to facilitate chemical reactions, such as acid-base catalysis or covalent catalysis.
- Cofactors and prosthetic groups: Many enzymes require additional non-protein components called cofactors or prosthetic groups for proper functioning. These small molecules assist in carrying out specific enzymatic reactions by providing necessary chemical functionalities.
Let’s now explore Methods for Measuring Enzyme Kinetics in detail to gain insight into experimental techniques employed in studying these fascinating biological catalysts.
Key Parameters in Enzyme Kinetics Analysis
Enzyme Kinetics: Classification of Enzymes
Transition from the previous section H2: Methods for Measuring Enzyme Kinetics
Having explored various methods for measuring enzyme kinetics, we will now delve into the classification of enzymes. To better understand the intricacies and functions of enzymes, let us consider an example.
Imagine a scenario where researchers are studying a novel enzyme found in extremophile microorganisms thriving in high-temperature environments such as hydrothermal vents deep within the ocean. This enzyme exhibits remarkable stability and catalytic activity even at elevated temperatures exceeding 100 degrees Celsius. By systematically investigating its characteristics through enzymatic assays, scientists aim to classify this unique enzyme based on its kinetic properties.
To classify enzymes effectively, several key parameters need to be considered:
- Substrate specificity: Each enzyme has a specific substrate with which it interacts and undergoes catalysis. The ability to discriminate between different substrates is crucial in defining an enzyme’s function.
- Reaction velocity: The rate at which an enzyme converts substrate into product is measured by reaction velocity. It provides valuable insights into how efficiently an enzyme carries out its catalytic activity.
- pH dependence: Enzymes often exhibit optimal activity at specific pH levels due to their sensitivity towards changes in hydrogen ion concentration. Understanding the pH dependence can aid in determining suitable conditions for enzymatic reactions.
- Temperature sensitivity: The effect of temperature on enzymatic activity plays a vital role in classifying enzymes. Different enzymes may have distinct temperature optima or operate over broad temperature ranges.
| Substrate Specificity | Reaction Velocity | pH Dependence | Temperature Sensitivity |
|---|---|---|---|
| Highly specific | Rapid | Acidic | Thermophilic |
| Moderate specificity | Moderate | Neutral | Mesophilic |
| Broad specificity | Slow | Alkaline | Psychrophilic |
In conclusion, understanding the classification of enzymes is crucial for comprehending their diverse functions and properties. By considering parameters such as substrate specificity, reaction velocity, pH dependence, and temperature sensitivity, researchers can categorize enzymes effectively. This knowledge lays a foundation for further investigations into enzyme kinetics and aids in elucidating enzymatic mechanisms.
Transition to subsequent section H2: Competitive Inhibition: Definition and Examples
Moving forward, we will explore competitive inhibition – an intriguing phenomenon that affects enzyme activity. Through the examination of various examples, we will gain insights into how this type of inhibition impacts enzymatic reactions without impeding progress.
Competitive Inhibition: Definition and Examples
Enzyme Kinetics: Classification of Enzymes
In the previous section, we explored the key parameters in enzyme kinetics analysis. Now, let us delve into an important aspect of enzyme classification and its implications in understanding enzymatic reactions. To make this topic more engaging, let’s consider a hypothetical example involving a commonly studied enzyme called lactase.
Lactase is responsible for breaking down lactose, a sugar found in milk and dairy products. Imagine studying the kinetic behavior of lactase by measuring its activity at different substrate concentrations. We observe that as the concentration of lactose increases, the rate of reaction also increases until it reaches a maximum value—a phenomenon known as saturation. This observation points to different modes of enzyme action, which can be classified based on how substrates interact with enzymes during catalysis.
To better understand the classification of enzymes, let’s examine four common types:
-
Michaelis-Menten Enzymes:
- Follow classic Michaelis-Menten kinetics.
- Exhibit hyperbolic substrate saturation curves.
- Display non-linear relationships between velocity and substrate concentration.
-
Allosteric Enzymes:
- Regulated by allosteric modulators (activators or inhibitors).
- Show sigmoidal substrate saturation curves.
- Possess multiple active sites that can bind substrates simultaneously.
-
Covalently Modified Enzymes:
- Undergo reversible covalent modifications (e.g., phosphorylation).
- Can switch between active and inactive states through modification.
-
Regulatory Enzymes:
- Control metabolic pathways by regulating key steps.
- Often subject to feedback inhibition from downstream metabolites.
Table 1: Comparison Between Different Types of Enzymes
| Type | Substrate Saturation Curve | Regulation Mechanism |
|---|---|---|
| Michaelis-Menten | Hyperbolic | No regulation |
| Allosteric | Sigmoidal | Allosteric modulation |
| Covalently Modified | Varies | Reversible modification |
| Regulatory | Varies | Feedback inhibition |
Understanding the classification of enzymes provides valuable insights into their mode of action and regulation. By studying lactase as an example, we can appreciate how different enzymes may exhibit distinct kinetic behaviors due to specific interactions with substrates or regulatory factors. This knowledge enables researchers to design targeted strategies for enzyme manipulation and intervention.
In the subsequent section on “Non-competitive Inhibition: Mechanisms and Significance,” we will explore another intriguing aspect of enzyme kinetics that involves a unique type of inhibition where inhibitors bind to sites distinct from the active site, altering enzyme activity in unexpected ways. So let us now delve deeper into this fascinating topic.
Non-competitive Inhibition: Mechanisms and Significance
Enzyme Kinetics: Classification of Enzymes
Competitive inhibition refers to a type of enzyme inhibition in which a molecule similar in structure to the substrate competes with the substrate for binding at the active site of the enzyme. This phenomenon can effectively reduce or prevent enzymatic activity, as it hinders the formation of enzyme-substrate complexes. An example of competitive inhibition is observed in the case of succinate dehydrogenase (SDH), an enzyme involved in cellular respiration. Malonate, a compound structurally resembling SDH’s substrate succinate, acts as a competitive inhibitor by competing with succinate for binding at the active site.
Non-competitive inhibition represents another mechanism through which enzymes are regulated. In this form of inhibition, the inhibitor binds to an allosteric site on the enzyme distinct from the active site. Consequently, it induces conformational changes that inhibit enzymatic activity even when substrate molecules are present. This type of regulation is exemplified by cyanide poisoning, where cyanide ions bind to cytochrome c oxidase, an important respiratory enzyme responsible for electron transfer during oxidative phosphorylation.
- Competitive inhibition occurs when a molecule competes with the substrate for binding at the active site.
- Non-competitive inhibition involves binding at an allosteric site and inducing structural changes that impede enzymatic activity.
- Both forms of inhibition affect reaction rates but do not alter Vmax values.
- Understanding these mechanisms is crucial for developing targeted drugs and designing effective therapies.
Moreover, let us examine how different types of inhibitors interact with enzymes by considering a table showcasing their characteristics:
| Type | Binding Site | Effect on Enzyme Activity |
|---|---|---|
| Competitive | Active site | Reduces enzymatic activity |
| Non-competitive | Allosteric site | Inhibits enzymatic activity |
Moving forward, we will explore the intriguing characteristics and applications of uncompetitive inhibition. This type of enzyme regulation involves binding to an allosteric site only after the substrate has bound to the active site, leading to unique functional consequences.
[Transition Sentence] As we delve into the topic of uncompetitive inhibition, let us uncover its distinctive traits and explore how it is utilized in various biological processes and industrial applications.
Uncompetitive Inhibition: Characteristics and Applications
Section H2: Non-competitive Inhibition: Mechanisms and Significance
Non-competitive inhibition is a key mechanism that affects enzyme kinetics. Unlike other types of inhibition, non-competitive inhibition occurs when the inhibitor binds to an allosteric site on the enzyme, which is distinct from the active site where the substrate normally binds. This type of inhibition does not directly interfere with the binding of the substrate but rather causes changes in enzyme conformation or prevents catalytic activity.
An intriguing example illustrating non-competitive inhibition involves the drug methotrexate and its target enzyme dihydrofolate reductase (DHFR). Methotrexate competitively inhibits DHFR by binding at its active site, preventing the conversion of dihydrofolate into tetrahydrofolate. However, it also exhibits non-competitive inhibition by binding to an additional allosteric site on DHFR. The dual mode of inhibition allows methotrexate to effectively reduce tetrahydrofolate levels within cells, making it a valuable chemotherapeutic agent for cancer treatment.
The significance of non-competitive inhibition lies in its ability to modulate enzymatic activity beyond mere competition for substrate binding sites. Here are some key points regarding non-competitive inhibition:
- Non-competitive inhibitors can bind both free enzymes and enzyme-substrate complexes.
- They do not affect the affinity between the enzyme and substrate.
- Non-competitive inhibitors decrease Vmax (maximum velocity) without altering Km (Michaelis constant).
- These inhibitors often exhibit structural similarities with substrates, allowing them to influence catalysis indirectly.
To further illustrate these concepts, consider Table 1 below showcasing examples of non-competitive inhibitors and their corresponding effects on enzymatic reactions:
Table 1: Examples of Non-Competitive Inhibitors
| Inhibitor | Enzyme | Effect |
|---|---|---|
| Aspirin | Cyclooxygenase | Inhibits prostaglandin |
| synthesis | ||
| Glyphosate | EPSP synthase | Blocks amino acid |
| biosynthesis | ||
| Ritonavir | HIV protease | Prevents viral |
| replication |
Non-competitive inhibition plays a crucial role in various biological processes and pharmaceutical applications. Understanding its mechanisms and significance provides valuable insights for drug design, enzyme regulation, and the development of therapeutic interventions.
Allosteric activation offers an alternative perspective on how enzymes can be regulated to enhance their activity and broaden their functional capabilities.
Allosteric Activation: Principles and Examples
Enzyme Kinetics: Classification of Enzymes
In the previous section, we explored the concept of uncompetitive inhibition in enzyme kinetics. Now, let us delve into the classification of enzymes based on their characteristics and applications.
One fascinating example that showcases the diversity of Enzyme Classifications is lactase. Lactase is an enzyme responsible for breaking down lactose, a sugar found in milk. This specific enzyme belongs to the hydrolase class, which catalyzes hydrolysis reactions by adding water molecules to break chemical bonds. Its classification further extends to carbohydrases since it specifically acts on carbohydrates like lactose. Understanding these classifications allows researchers to identify enzymes with similar properties and functions, aiding in various practical applications.
To provide a more comprehensive understanding, here are some key points regarding enzyme classification:
- Oxidoreductases: These enzymes facilitate oxidation-reduction reactions by transferring electrons between substrates.
- Transferases: They transfer functional groups from one molecule to another.
- Hydrolases: As mentioned earlier, they catalyze hydrolysis reactions by adding water molecules.
- Lyases: Lyases cleave or form double bonds without utilizing water as a substrate.
Let’s now take a closer look at how these classifications can be summarized in a table format:
| Class | Example | Reaction Type |
|---|---|---|
| Oxidoreductases | Alcohol dehydrogenase | Oxidation-reduction |
| Transferases | Transaminase | Group transfer |
| Hydrolases | Lipase | Hydrolysis |
| Lyases | Decarboxylase | Addition/elimination |
As we conclude this section on the classification of enzymes, it becomes evident that categorizing them according to their properties plays a crucial role in studying their functions and developing practical applications. This understanding forms the foundation for further exploration of enzyme kinetics, particularly in relation to cooperativity.
Cooperativity in Enzyme Kinetics: Insights and Implications
In the previous section, we explored the fascinating concept of allosteric activation in enzymes. Now, let us delve into another important aspect of enzyme kinetics – cooperativity. Cooperativity refers to the phenomenon where binding of a substrate to one active site on an enzyme influences the activity of other active sites within the same enzyme molecule. This intricate interplay between multiple subunits or domains can significantly impact enzymatic function.
To illustrate this concept, consider hemoglobin, a protein responsible for oxygen transport in our red blood cells. Hemoglobin exhibits cooperative binding behavior towards oxygen molecules. As more oxygen binds to one heme group within the hemoglobin tetramer, it induces conformational changes that promote further oxygen binding at other heme groups. Likewise, when oxygen is released from one heme group, it triggers a cascade of conformational changes leading to rapid release of remaining bound oxygen molecules. This cooperative behavior ensures efficient loading and unloading of oxygen during gas exchange in tissues.
The following bullet points highlight key features and implications of cooperativity:
- Cooperative enzymes exhibit sigmoidal (S-shaped) velocity-substrate concentration curves instead of hyperbolic ones seen for non-cooperative enzymes.
- Positive cooperativity enhances substrate affinity as additional substrates bind, while negative cooperativity reduces substrate affinity.
- Cooperativity allows fine-tuning enzyme activity based on varying concentrations of substrates or regulatory molecules.
- Understanding cooperativity is crucial for designing drugs that modulate enzyme function by targeting allosteric sites.
Now let’s explore the table below which summarizes some well-known examples of cooperative enzymes:
| Enzyme | Substrate | Type |
|---|---|---|
| Hemoglobin | Oxygen | Positive |
| Adenosine deaminase | Adenosine | Negative |
| Phosphofructokinase | Fructose-6-phosphate | Positive |
| Aspartate transcarbamoylase | Carbamoyl phosphate | Negative |
As we conclude our discussion on cooperativity, it is important to note that this phenomenon adds an additional layer of complexity to enzyme kinetics. The interplay between multiple active sites within enzymes can greatly influence their catalytic efficiency and regulatory properties. In the subsequent section, we will explore another fundamental concept in enzymology – the Michaelis-Menten equation.
Michaelis-Menten Equation: Derivation and Limitations
Transitioning from the discussion on cooperativity in enzyme kinetics, we now delve into the classification of enzymes. Understanding how enzymes are classified provides valuable insights into their diverse functions and catalytic mechanisms. Additionally, this knowledge enables researchers to better comprehend the complexities of enzymatic reactions, leading to practical applications such as drug development and biotechnological advancements.
To illustrate the significance of enzyme classification, let us consider an example involving a hypothetical enzyme called “Xylanase-A.” Xylanases are enzymes that break down xylan, a complex polysaccharide found in plant cell walls. In our case study, Xylanase-A exhibits cooperative behavior in its catalytic activity. By studying its classification, we can gain further understanding of how this enzyme interacts with its substrate and how it is regulated within a biological system.
Enzymes are categorized based on various criteria, including their mode of action and specificity towards substrates. Here are some key points regarding enzyme classification:
- Enzyme Commission (EC) numbers: The EC system assigns unique numerical identifiers to each known enzyme based on their specific reaction types. This standardized nomenclature facilitates communication among scientists worldwide.
- Oxidoreductases: This group consists of enzymes involved in oxidation-reduction reactions. They play crucial roles in energy metabolism and cellular respiration.
- Hydrolases: These enzymes facilitate hydrolysis reactions by breaking chemical bonds through the addition of water molecules. Examples include proteases that degrade proteins and lipases that break down lipids.
- Transferases: Transferases transfer functional groups between molecules, facilitating important biochemical processes like DNA replication and protein synthesis.
In summary, understanding the classification of enzymes allows for a comprehensive analysis of their diverse functionalities and regulatory mechanisms. Through concrete examples like Xylanase-A, researchers can explore the implications of different classifications on an enzyme’s behavior and function. By expanding our knowledge in this area, we open doors to novel applications and advancements in fields such as medicine, agriculture, and biotechnology.
| Enzyme Classification | Examples | Mode of Action |
|---|---|---|
| Oxidoreductases | Alcohol dehydrogenase | Facilitate oxidation-reduction |
| reactions | ||
| Hydrolases | Chymotrypsin | Catalyze hydrolysis reactions |
| by adding water molecules | ||
| Transferases | DNA polymerase | Transfer functional groups |
| between molecules |
Please note that the emotions evoked by the bullet point list and table may vary depending on the reader’s background and personal interests.