Scribd Logo
Upload

Welcome to Scribd!

  • 50 views

    Nguyen Thi Ngoc Linh - Enzymology

    Uploaded by

    LinhNguye
    This document discusses how enzymes are categorized and the nature of enzyme-substrate interactions. It describes the six main categories of enzymes based on the chemical reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then elaborates on how enzymes interact with substrates, including through cofactors, coenzymes, activators, and competitive and non-competitive inhibitors. Finally, it provides reasons for the lock-and-key and induced-fit models of enzyme-substrate interaction, noting enzymes and substrates must have complementary shapes to efficiently catalyze reactions under mild cellular conditions.

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd

    Nguyen Thi Ngoc Linh - Enzymology

    Uploaded by

    LinhNguye
    50 views4 pages
    This document discusses how enzymes are categorized and the nature of enzyme-substrate interactions. It describes the six main categories of enzymes based on the chemical reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then elaborates on how enzymes interact with substrates, including through cofactors, coenzymes, activators, and competitive and non-competitive inhibitors. Finally, it provides reasons for the lock-and-key and induced-fit models of enzyme-substrate interaction, noting enzymes and substrates must have complementary shapes to efficiently catalyze reactions under mild cellular conditions.

    Original Title

    Nguyen Thi Ngoc Linh - enzymology

    Copyright

    © © All Rights Reserved

    Available Formats

    DOCX, PDF, TXT or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    This document discusses how enzymes are categorized and the nature of enzyme-substrate interactions. It describes the six main categories of enzymes based on the chemical reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then elaborates on how enzymes interact with substrates, including through cofactors, coenzymes, activators, and competitive and non-competitive inhibitors. Finally, it provides reasons for the lock-and-key and induced-fit models of enzyme-substrate interaction, noting enzymes and substrates must have complementary shapes to efficiently catalyze reactions under mild cellular conditions.

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    50 views4 pages

    Nguyen Thi Ngoc Linh - Enzymology

    Uploaded by

    LinhNguye
    This document discusses how enzymes are categorized and the nature of enzyme-substrate interactions. It describes the six main categories of enzymes based on the chemical reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. It then elaborates on how enzymes interact with substrates, including through cofactors, coenzymes, activators, and competitive and non-competitive inhibitors. Finally, it provides reasons for the lock-and-key and induced-fit models of enzyme-substrate interaction, noting enzymes and substrates must have complementary shapes to efficiently catalyze reactions under mild cellular conditions.

    Copyright:

    © All Rights Reserved
    Download as DOCX, PDF, TXT or read online from Scribd
    Download as docx, pdf, or txt
    of 4

    Nguyễn Thị Ngọc Linh

    BTBCIU17041
    ENZYMOLOGY

     Question 1 : How enzymes are categorized into different classes and types ?
    Enzymes are classified into six categories which based on the type of chemical reaction
    catalyzed.

    1) Oxidoreductases :
    This group including two types of reactions ( oxidation and reduction ). These reactions
    involve the transfer of electron, hydrogen or oxygen atom. There are 22 subclasses of oxido-
    reductases. These enzyme can catalyze both the forward and reverse reaction.
    Example: the dehydrogenases that oxidize Pyruvate by transferring hydrorgen atoms to a
    coenzyme NAD+ that act as an acceptor.
    Pyruvate + NADH  Lactic Acid + NAD+

    2) Transferases
    Tranferases are enzymes responsible for transferring a functional group from a donor to a
    suitable acceptor. Tranferases need coenzymes, and they are surely intracellular. There are
    nine subgroups of tranferases that can be differentiated according to the group that is being
    moved. In cell metabolism, the most important group are methyltranferases, acytranferases,
    glycolsyltransferases, transaminase, and phosphotranferases.
    Example:
    Glucose + ATP → Glucose 6-P + ADP

    3) Hydrolase
    Hydrolases take responsibility for catalysis of bond cleavage by reacting with water. Most of
    hydrolases do not require cofactors to catalyze reactions, many are extracellular, and accept
    the addition of water-miscible solvent. According to the differences in the types of susceptible
    bond, there are 12 subclasses of hydrolases. The enzymes belongs to this category are able
    to catalyze reverse reaction of bond formation with water elimination, under proper conditions.
    Example:
    Glucose 6-P + H20 → Glucose + Pi

    4) Lyases
    Lyases are enzymes acting on the cleavage of chemical bond that are not hydrolytic or
    oxidative. This reaction often results in the formation of a new cyclic structure or a new double
    bond. Corresponding to their type of susceptible bond, the enzymes of this class are divided
    into seven subclasses: C-C, C-O, C-N, C-X ( halides), C-S, P-O, and other bond. Most of
    these enzymes are intracellular, some of them do not require coenzymes and perform
    different metabolic functions associated with cell catabolism and biosynthesis, by acting in a
    reverse mode.
    Example:
    Fumarate + H20  L-malate

    5) Isomerase
    This class of enzymes are able to catalyze reactions such as racemization and epimerization.
    Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed.
    There are six subclasses of isomerases based on the type of isomer produced: racemases
    and epimerases; cis–trans-isomerases, intramolecular oxidoreductases, intramolecular
    transferases (mutases), intramolecular lyases and other isomerases. Most isomerases are
    intracellular and some of them work with necessary requirement of cofactor.
    Example:
    UDP- Glucose → UDP- Glactose
    6) Ligases
    Ligases are enzymes that are capable of catalyzing the reaction of joining two large
    molecules by establishing a new covalent bond. These enzymes responsible for cell
    anabolism and as such perform an essential role in the reactions of synthesis inside the cell
    (sometimes they are named synthetases). There are six subgroups of ligases according to
    the type of bond formed: C-O, C-S, C-N, C-C, phosphoric esters and C-metal. Ligases are
    complex high molecular weight strictly intracellular coenzyme requiring enzymes. The
    reaction of synthesis is frequently coupled with the hydrolysis of an energy rich bond, as in
    ATP or other energy rich containing triphosphates.
    Example:
    Pyruvate + CO2 + ATP + H20  oxaloacetate + ADP + Pi

    Question 2: Elaborate on the nature of the interactions between enzymes and the
    corresponding substrates (i.e. what kinds of possible interaction between them).
    Enzymes are biological catalysts (typically proteins) that within the mild conditions of
    temperature, pH, and pressure of the cells, accelerate the rates of such reactions by well over
    a million-fold without itself being consumed or altered. They are characterized by a
    remarkable efficiency and specificity.
    Enzyme can be controlled by regulatory molecule that either increase or decrease the activity
    of them. Molecules which enhance the enzymes’ activity are called activators, while others
    reduce the activity of enzymes are called inhibitors.
    - Activator -
    If enzymes bound to non-protein helper molecule which are cofactors and coenzymes, they
    would function optimally.
    Ÿ Cofactors:
    Some enzymes require cofactors which are inorganic ions to work properly. Cofactors may be
    attached temporarily to the enzyme through ionic or hydrogen bonds, or permanently through
    stronger covalent bonds.
    → For instance, DNA polymerase requires a zinc ion (Zn2+) to build DNA molecules. 
    Ÿ Coenzymes:
    Other enzyme need coenzymes that are organic molecule ( carbon-based ). Vitamins are
    known as a great source of coenzymes. Some vitamins are precursors to coenzymes and
    others act directly as coenzymes.
    → For example, vitamin B12, or cobalamin, are modified to become the coenzymes
    methylcobalamin and deoxyadenosylcobalamin. These coenzymes are required in the
    enzymes which change homocysteine to methionine.

    - Inhibitors -
    An inhibitor is a substance that reversibly interacts with the enzyme reducing its catalytic
    potential.
    According to the catalytic step with which they interact, inhibitors are categoried into 2 types:
    Ÿ Competitive inhibitor is a molecule which is similar enough to a substrate that it can bind
    to the enzyme’s active site to stop it from binding to the substrate.
    Ÿ Non-competitive inhibitors attaches at another site ( allosteric site) and blocks the
    enzyme from doing its job.The substrate can still bind to the enzyme at the active site, but the
    inhibitor changes the shape of the enzyme so it is no longer in optimal position to catalyze the
    reaction.

    Question 3: provide reasons explaining why nature decided the nature of the enzyme-
    substrate interaction
    Under very mild conditions of temperature and pH, enzymes catalyze essentially all of the
    thousands of metabolic reactions tremendously which taking place in cells. Acting in
    organized sequences, they catalyze the hundreds of stepwise reactions that degrade nutrient
    molecules, conserve and transform chemical energy, and make biological macromolecules
    from simple precursors.
    A simple enzymatic reaction
    E + S ↔ ES ↔ EP ↔ E + P
    There are two models for enzyme-substrate interaction : lock and key, induced fit model.
    Ÿ In lock and key model, the enzyme is the lock and the substrate is the key. As with a lock
    and the key that opens it the shapes must be complementary and this shape can not change.
    Ÿ Induced fit looks at the active site of enzymes as being slightly more flexible and initially
    uncomplementary.

    You might also like