Biochem

1. An enzyme is a compound, usually a protein, that acts as a catalyst for a biochemical reaction. Enzymes cause cellular
reactions to occur millions of times faster than corresponding uncatalyzed reactions. Enzymes undergo all the reactions of
proteins, Slight alterations in pH or temperature affect enzyme activity dramatically.

2. Enzymes can be divided into two general structural classes: simple enzymes and conjugated enzymes. A conjugated enzyme
is an enzyme that has a nonprotein part in addition to a protein part, while A simple enzyme is an enzyme composed only of
protein (amino acid chains). An apoenzyme is the protein part of a conjugated enzyme. A cofactor is the nonprotein part of a
conjugated enzyme. These enzymes are all involved in growth, blood coagulation, healing, reproduction and other biological
activities.

3. Enzymes are most commonly named by using a system that attempts to provide information about the function (rather than
the structure) of the enzyme. Three important aspects of the enzyme-naming process are the following:
1. The suffix -ase identifies a substance as an enzyme. Thus urease, sucrase, and
lipase are all enzyme designations. The suffix -in is still found in the names of
some of the first enzymes studied, many of which are digestive enzymes. Such
names include trypsin, chymotrypsin, and pepsin.
2. The type of reaction catalyzed by an enzyme is often noted with a prefix.
An oxidase enzyme catalyzes an oxidation reaction, and a hydrolase enzyme
catalyzes a hydrolysis reaction.
3. The identity of the substrate is often noted in addition to the type of reaction.
Enzyme names of this type include glucose oxidase, pyruvate carboxylase, and
succinate dehydrogenase. Infrequently, the substrate but not the reaction type is
given, as in the names urease and lactase. In these names, the reaction involved is
hydrolysis; urease catalyzes the hydrolysis of urea, lactase the hydrolysis of lactose.

4. Enzymes are grouped into six major classes on the basis of the types of reactions
they catalyze, and they include:

An oxidoreductase is an enzyme that catalyzes an oxidation–reduction reaction. an oxidoreductase requires a

coenzyme that is oxidized or reduced as the substrate is reduced or oxidized.
Lactate dehydrogenase is an oxidoreductase that removes hydrogen atoms from
a molecule.

A transferase is an enzyme that catalyzes the transfer of a functional group from one molecule to another. Two major subtypes
of transferases are transaminases and kinases. A transaminase catalyzes the transfer of an amino group from
one molecule to another.

A hydrolase is an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the
bond to break. Hydrolysis reactions are central to the process of digestion.

A lyase is an enzyme that catalyzes the addition of a group to a double bond or the
removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation.

An isomerase is an enzyme that catalyzes the isomerization (rearrangement of atoms) of a substrate in a reaction, converting it
into a molecule isomeric with itself. There is only one reactant and one product in reactions where isomerases
are operative.

A ligase is an enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP.

5. The lock and key model requires binding of specific substrate before they can catalyze a chemical reaction, this is because
enzymes are highly specific. While the induced-fit model is where a small change can happen in order for a substrate and an
active site to be ideally fit for catalysis.

6 . Enzyme specificity is the extent to which an enzyme’s activity is restricted to a specific substrate,
a specific group of substrates, a specific type of chemical bond, or a specific type of
chemical reaction. Types of enzyme specifity include :

Absolute specificity—the enzyme will catalyze only one reaction. This most
restrictive of all specificities is not common.
Group specificity—the enzyme will act only on molecules that have a specific functional group, such as hydroxyl, amino, or
phosphate groups.

Linkage specificity—the enzyme will act on a particular type of chemical bond, irrespective of the rest of the molecular structure.
Linkage specificity is the most general of the common specificities.

Stereochemical specificity—the enzyme will act on a particular stereoisomer. Chirality is inherent in an enzyme active site
because amino acids are chiral compounds.

7 . Enzyme activity is a measure of the rate at which an enzyme converts substrate to products in a biochemical reaction. Factors
that affect enzyme activity include temperature, pH, substrate concentration, and enzyme concentration.

8. Enzymes has a lot of medical capabilities, Several common types of prescription drugs have modes of action that involve
enzyme inhibition. Included among them are ACE inhibitors, sulfa drugs, and penicillins. ACE or angiotensin-converting enzyme
is involved in blood pressure regulation. sulfa drugs—the first “antibiotics” in the medical field. Antibiotics exert their action
selectively on bacteria and do not affect the normal metabolism of the host organism. Antibiotics usually inhibit specific enzymes
essential to the life processes of the bacteria.Penicillin is also one of the most widely used antibiotics, Penicillins inhibit
transpeptidase, an enzyme that catalyzes the formation of peptide cross-links between polysaccharide strands in bacterial cell
walls. These crosslinks strengthen cell walls. Enzymes are also used in clinical laboratory chemical analysis.

9 .A vitamin is an organic compound, essential in small amounts for the proper functioning of the human body, that must be
obtained from dietary sources because the body cannot synthesize it. Vitamins are considered in conjunction with enzymes
because many enzymes contain vitamins as part of their structure. Vitamins also also fall into two categories: fat soluble and
water solubles.

10 . Water-soluble vitamins function as coenzymes for a number of important biochemical reactions in humans, animals, and
microorganisms. Fat-soluble vitamins generally do not function as coenzymes in humans and animals and are
rarely utilized in any manner by microorganisms. Water soluble vitamins include Vitamin C and the B vitamins. Vitamin C exists
in two active forms in the human body: an oxidized form and a reduced form. Human beings, primates and other animals
cannot biosynthesize the compound and, hence, must obtain it from dietary intake. Important biochemical functions for vitamin
C in the human body include the following: Collagen Synthesis, General Antioxidant, and Synthesis of Nuerotransmitters. On the
other hand, the B vitamins include: Thiamin, Riboflavin, Niacin, Pantothenic acid, Vitamin B6, Biotin, Folate and Vitamin B12. B
vitamins help the body convert food into energy, maintain skin and brain cells, create new blood cells and other body tissues.

Fat- soluble vitamins include Vitamins A, D, E, and K.Many of the functions of the fat-soluble vitamins involve processes that
occur in cell membranes. The structures of the fat-soluble vitamins are more hydrocarbon-like, with fewer functional groups
than the water-soluble vitamins. Vitamin A has four major functions in the body: Vision, Regulating cell differentiation,
maintenance of the Health of Epithelial Tissues, and Reproduction and Growth.Second, Vitamin D, like vitamin A, exists in
several forms, The principal function of vitamin D is to maintain normal blood levels of calcium ion and phosphate ion so that
bones can absorb these ions. Vitamin D stimulates absorption of these ions from the gastrointestinal tract and aids in their
retention by the kidneys.Third, Vitamin E which has four forms: alpha-, beta-, delta-, and gamma-tocopherol.The primary
function of vitamin E in the body is as an antioxidant—a compound that protects other compounds from oxidation by being
oxidized itself. Vitamin E is particularly important in preventing the oxidation of polyunsaturated fatty acids
in membrane lipids. Lastly, Vitamin K is essential to the blood-clotting process, it is also essential for the formation of
prothrombin and at least five other proteins involved in the regulation of blood clotting. Vitamin K is sometimes given to
presurgical patients to ensure adequate prothrombin levels and to prevent hemorrhaging. Vitamin K is also required for the
biosynthesis of several other proteins found in the plasma, bone, and kidney.