This document discusses the nomenclature and classification of enzymes. It explains that enzymes are typically named based on the substrate they act upon or the type of reaction they catalyze. The International Union of Biochemistry developed a systematic classification system for enzymes based on the chemical reaction catalyzed. This system divides enzymes into six major classes and provides a four-digit Enzyme Commission number for each enzyme to uniquely identify it. The six major classes are oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
A lipid is chemically defined as a substance that is insoluble in water and soluble in alcohol, ether, and chloroform. Lipids are an important component of living cells. Together with carbohydrates and proteins, lipids are the main constituents of plant and animal cells. Cholesterol and triglycerides are lipids.
A lipid is chemically defined as a substance that is insoluble in water and soluble in alcohol, ether, and chloroform. Lipids are an important component of living cells. Together with carbohydrates and proteins, lipids are the main constituents of plant and animal cells. Cholesterol and triglycerides are lipids.
Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
HISTRY
The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
Properties of allosteric enzyme
Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
A comprehensive presentation on Enzymology :Types of Enzyme inhibition & Therapeutic uses for MBBS ,BDS, B Pharm & Biotechnology students to facilitate self- study.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
HISTRY
The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
Properties of allosteric enzyme
Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
A comprehensive presentation on Enzymology :Types of Enzyme inhibition & Therapeutic uses for MBBS ,BDS, B Pharm & Biotechnology students to facilitate self- study.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes
Enzymology , classification of enzymes, coenzymesAkhil Pradeep
LDH
AST
ALT
GGT
Troponin
PSA
ALP
Heart isoenzymes
Liver isoenzymes
CKMB include all but not limited to following details normal value... interpretation ,Estimation, Co enzymes
Enzymology , classification of enzymes, coenzymesAkhil Pradeep
Enzymology TEXTBOOK OF
BIOCHEMISTRY by D M vasudevan, sreekumari and kannan vaidya narayanan
Biochemistry by u satyanarayanan.
Prepare study note (1500words) from above text book for detailed research purposes on clinical enzymology. Note nees to be so detailed it should include all all topic sub topic and further related topic to make a comprehensive study note. Include as many details as possible. Include following but no limited to following details Sub heading
LDH
AST
ALT
GGT
Troponin
PSA
ALP
Heart isoenzymes
Liver isoenzymes
CKMB include all but not limited to following details normal value... interpretation ,Estimation, Co enzymes
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The people of Punjab felt alienated from main stream due to denial of their just demands during a long democratic struggle since independence. As it happen all over the word, it led to militant struggle with great loss of lives of military, police and civilian personnel. Killing of Indira Gandhi and massacre of innocent Sikhs in Delhi and other India cities was also associated with this movement.
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Published classroom materials form the basis of syllabuses, drive teacher professional development, and have a potentially huge influence on learners, teachers and education systems. All teachers also create their own materials, whether a few sentences on a blackboard, a highly-structured fully-realised online course, or anything in between. Despite this, the knowledge and skills needed to create effective language learning materials are rarely part of teacher training, and are mostly learnt by trial and error.
Knowledge and skills frameworks, generally called competency frameworks, for ELT teachers, trainers and managers have existed for a few years now. However, until I created one for my MA dissertation, there wasn’t one drawing together what we need to know and do to be able to effectively produce language learning materials.
This webinar will introduce you to my framework, highlighting the key competencies I identified from my research. It will also show how anybody involved in language teaching (any language, not just English!), teacher training, managing schools or developing language learning materials can benefit from using the framework.
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3. • 1) Enzyme acted upon the substrate
: The molecule upon which enzyme
acts is known as substrate. Naming
of an enzyme by adding the suffix –
ase in the name of the substrate
which is catalyzed by the enzyme.
For example, enzymes catalyzing
lipids were named lipases, nucleic
acids as nucleases and so on……
• A few of the names were even more
specific like maltase (acting upon
maltose), tyrosinase (tyrosine),
sucrase (sucrose) etc.,
NOMENCLATURE AND CLASSIFICATION
4. • 2). Type of reaction catalyzed by enzyme :
The enzymes are highly specific to the reaction they catalyze. Hence,
this has been necessary in naming them by adding suffix- ase in the
name of the reaction; for example hydrolases (catalyzing hydrolysis),
isomerases (isomerization), oxidases (oxidation), dehydrogenases
(dehydrogenation), transaminases (transamination), Phosphorylases
(phosphorylation) etc.,
5. • Although these two systems are quite simple and easy to follow, there
are certain discrepancies present in them. The former system does
not take into account the type of the reaction catalyzed, whereas in
the latter system no idea can be derived regarding the nature of the
substrate acted upon by the enzyme.
6. • 3). Substrate acted upon and type of reaction catalyzed :
• The names of some enzymes give clue of both the substrate utilized
and the type of reaction catalyzed. For example, the enzyme succinic
dehydrogenase catalyzes the dehydrogenation of the substrate
succinic acid.
• Similarly, L-glutamic dehydrogenase indicates an enzyme catalyzing a
dehydrogenation reaction involving L-glutamic acid.
7. • 4). Substance that is synthesized :
• A few enzymes have been named by adding the suffix –ase to the
name of the substance synthesized, viz., fumarase that forms
fumarate irreversibly from L-malate.
8. • 5). Chemical composition of the enzyme :
• Based on their chemical composition, the enzymes have been
classified into following categories:
• a). Enzyme molecule consisting of protein only- e.g., pepsin, trypsin,
urease, papain, amylase etc.,
• b). Enzyme molecule containing a protein and a cation- e.g., carbonic
anhydrase (containing Zn2+ as cation), arginase (Mn2+ ), tyrosinase
(Cu2+) etc.
• c). Enzyme molecule containing a protein and a nonprotein organic
compound known as prosthetic group-.
9. On the basis of the nature of prosthetic group present these
enzymes has been subdivide into:
• i). Iron porphyrin enzymes- catalase, cytochrome c peroxides I and II.
• Ii). Flavoprotein enzymes- glycine oxidase, pyruvate oxidase,
histamine.
• Iii). Diphosphothiamin enzymes- β-carboxylase, pyruvate mutase.
• Iv). Enzymes requiring other coenzymes- Phosphorylase, amino acid
decarboxylase.
13. Over-allchemicalreactiontakeninto
consideration
• The chemical reaction catalyzed is the specific property which
distinguishes one enzyme from another. In 1961, International Union
of Biochemistry (I.U.B.) used this criterion as a basis for the
classification and naming of enzymes. Although complicated, the
I.U.B. system is precise, descriptive and informative.
14. The major features of this system of classification of enzymes are as
follows:
• (a) The reactions and the enzymes catalyzing them are divided into 6 major
classes, each with 4 to 13 subclasses.
• (b) Each enzyme name has two parts- the first part is the name of the substrate
and the second part which ends in suffix –ase, indicates the type of the reaction
catalyzed.
• (c) Additional information regarding the nature of the reaction, if needed,is given
in parenthesis.
• For example, the enzyme malate dehydrogenase catalyzes the following reaction:
• L-malate + NAD+ Pyruvate +CO2 + NADH + H+
15. • (d) Each enzyme has been allotted a systemic code number called Enzyme
Commission (E.C.) number. The E.C. number for each enzyme consists of a series
of numbers at 4 places:
• the first place numbers representing the major class to which enzyme belongs,
the two median numbers denoting the subclass and the sub-subclass of the
enzyme within the major class. The last place number or the fourth digit
represents the serial number of the enzyme within the sub-subclass.
• Thus E.C.2.7.1.1 represents class 2 (a transferase), subclass 7 (transfer of
phosphate), sub-subclass 1 (an alcohol group as phosphate acceptor). The final
digit denotes the enzyme, hexokinase or ATP:
• D-hexose-6-phosphotransferase. This enzyme catalyzes the transfer of phosphate
from ATP to the hydroxyl group on carbon 6 of glucose.
• ATP + D-hexose hexokinase ADP+ Hexose-6-phosphate
16. • (e) Where no specific category has been created for an enzyme, it is
listed with a final figure of 99 in order to leave space for new
subdivisions. For example, 4.2.99 refers to “other carbon-oxygen
lyases.”
17. • The 6 major classes of enzymes with some important examples from some
subclasses are given below:
• 1. oxidoreductases:
• This class comprises the enzymes which were earlier called dehydrogenases,
oxidases, peroxidases, hydroxylases, oxygenases etc. The group includes those
enzymes which bring about oxidation-reduction between two substrates, A and B.
• 2. Transferases:
• Enzymes which catalyze the transfer of a group, G between a pair of substrates, A
and B are called transferases.
• In these are included the enzymes catalyzing the transfer of one carbon groups,
aldehydic or ketonic residues and phosphorus or sulfur-containing goups.
18. • 3. hydrolases:
• These catalyze the hydrolysis of their substrates by adding
constituents of water across the bond they split.
• 4.lyases(=Desmolases):
• These are those enzymes which catalyze the removal of groups from
substrates by mechanisms other than hydrolysis, leaving double
bonds.
• 5. Isomerases:
• these catalyze interconversions of optical, geometric or positional
isomers by intramolecular rearrangements of atoms or groups.
19. • 6. Ligases: (ligare= to bind) or synthetases:
• These are enzymes catalyzing the linking together of two compounds
utilizing the energy made available due to simultaneous breaking of a
pyrophosphate bond in ATP or a similar compound.