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BIO503 MIDTERM PAST PAPERS SARGODHA UNIVERSITY
BIO503 MIDTERM PAST PAPERS SARGODHA UNIVERSITY
CS201 FINAL TERM SOLVED PAPERS BY WAQAR SIDHU. ENG101 FINAL TERM SOLVED MCQS. CS403 CURRENT FINAL TERM PAPERS. CS101 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS201 FINAL TERM SOLVED PAPERS BY MOAAZ MEGA FILE. CS205 FINAL TERM PAST PAPERS. CS204 FINAL TERM PAST PAPERS. CS301 FINAL TERM SOLVED PAPERS BY MOAAZ. CS304 FINAL TERM SOLVED PAPERS BY MOAAZ. CS311 FINAL TERM SOLVED PAPERS BY MOAAZ. CS401 FINAL TERM SOLVED PAPERS BY MOAAZ
If two amino acids are to be made a
Peptide bond, a carboxyl group and an amino group
There must be other sites of conflict. when activated
The base of the enzyme binds to amino acids, however
Second amino. was held in the correct orientation to respond to
acid when the substrate binds to the enzyme.
Enzymes induce stress in the suprate. one leg molecule
Due to the binding of the enzyme bond to the active site
substrate to stretch, putting it in an unstable transition
For example, polysaccharide molecules
The enzyme lysozyme enters the active site in a flat ring
“chair” shape, but the active platform quickly flattens it
Show on a “couch”
As its bonds grow, they shrink
Stable and highly reactive to enzymes
Other substrate, water.
Enzymes temporarily add chemical groups
Subject. Side Chain (R Group)
Amino acids of an enzyme may be direct participants in the production of additional substrates.
For example, in an acid base
Catalyst, edge acid or primary chain
The amino acids forming the active site can be
transfer H+ to the substrate or space, disrupt a covalent bond in the substrate and
It is allowed to break. In a covalent reaction, a
The display panel in the side chain forms a temporary covalent bond with a component
In substrate metal ion catalysis, the metal ion
copper, zinc, iron and manganese,
are tied tightly to the edge chains
Proteins can lose or gain electrons without
Separation from proteins. BIO503 MIDTERM PAST PAPERS SARGODHA UNIVERSITY
This ability causes them to participate in antioxidant reactions – reduction,
It involves the loss or presence of electrons as determined by the molecular structure.
Most enzymes (and ribosomes) are larger than
leg molecule An enzyme is a protein usually consisting of hundreds of amino acids and may contain a fold
Polypeptide chain or several subgroups. Its substrate is usually a small molecule. The active portion of the enzyme is usually relatively small, no more than 6-12 amino acids.
Two questions arise from this observation:
what is the nature of the active site that allows it
Identify and bind substrate?
What is the role of the remaining large proteins?
Active Site Substrate -Specified
The critical ability of an enzyme to be selected correctly
The exact substrate depends on the precise interaction of the molecular forms and the interaction of the chemical groups at the binding site. The binding of the foundation to the active site depends on the same type of forces that maintain the tertiary level.
Enzyme Structure: Hydrogen Bonds, Gravity and
Separation of electrically charged groups, and hydrophobic
In 1894, German chemist Emil Fischer compared
fits into a lock between an enzyme and its substrate and
The pattern of the main fissure continues for more than half a century
With only indirect evidence to support it. The first direct evidence came from David Phillips and his colleagues in 1965.
succeeded in crystallization at the Royal Company in London
The enzyme determines the lysozyme and its tertiary structure
Using X-ray crystallography techniques (described
Chapter 11). They took good care of a pack of lysozyme
Its base corresponds to the substrate.
An enzyme changes shape when it binds to a substrate
As with proteins, enzymes do not change structures. as it is
Egg white protein structure changes when egg is present
hot, many enzymes change their structure (even less
especially) when they bind to their substrates.
Changes in shape expose the active sites – parts of the enzyme – that actually react to the substrate. one such
Enzyme shape changes due to substrate binding
called induced fit.
Induced compatibility is found with the enzyme hexokinase
while reading it with and without
The leg molecule, glucose (the other substrate is ATP).
Glucose + ATP → Glucose 6-phosphate + ATP
The induced fit aligns and accelerates the reaction side chain with the substrate from the enzyme’s active site
The catalytic mechanism described earlier (see Fig. 6.12).
Equally important, the hexogeneous fold
There is no water from the active site in the glucose substrate. This
important, because the two molecules actively bind
The site is glucose and ATP. If there is water, then ATP can do this
Dehydrated with ATP and phosphate. But in the absence of water, phosphate is converted from ATP to glucose
The induced fit partly explains why such enzymes are
The larger remaining macromolecule may play two roles:
It provides a structure for amino acids.
The active site is related to the substrate.
This participates in small but significant changes in the shape and structure of proteins, resulting in induced fit.
Some enzymes require other molecules
No matter how large and complex the enzymes are, many of them are needed
To function, the presence of other non-protein molecules. Some molecular “partners” are:
Cafactor These are mineral ions such as copper and zinc.
or binding iron with certain enzymes and essential
Coenzyme. carbon containing molecule
Required for the activation of one or more enzymes.
Coenzymes are usually relatively small in comparison
They are enzymes that temporarily bind.
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