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Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... The key problems: The structure of protein amino acids. The classification of amino acids according to both the polarity and the structural features of their side chains (e. g. polar, nonpolar; aliphatic, aromatic; sulfur-containing; charged, uncharged; acidic, basic). The amphoteric properties of a ...
Biochemistry Biochemistry is a science concerning the chemical
Biochemistry Biochemistry is a science concerning the chemical

... The formation, structure and properties of the peptide bond. Some important peptides in the human organism (glutathione, peptide hormones). The insulin synthesis. The classification of proteins according to their structure, properties and functions. The characteristics of primary, secondary, tertiar ...
Chapter 7: Recent advances in enzyme technology
Chapter 7: Recent advances in enzyme technology

... initially formed. Under normal physiological conditions, hydrolytic enzymes catalyse the degradation of polymers; i.e. hydrolases are transferases normally transferring a moiety to the acceptor, water. Water is normally present in a vast molar excess over other potential acceptor molecules so no rea ...
22. Think of two different proteins: both are enzymes. a) What
22. Think of two different proteins: both are enzymes. a) What

... Both molecules (E & N) in this case are negative effectors/allosteric inhibitors. Molecule N will inhibit Enz5, but because Enz1 is more of a secondary step, molecule E will have the most effect on Enz2 because it is the first step in the pathway that is unique. 43. PFK is an enzyme that catalyzes ...
2. Organic Compounds and the Four Biomolec
2. Organic Compounds and the Four Biomolec

... amino group (which is basic) and an acid group. Proteins consist of long chains of amino acids, with the acid group of one bonded to the amino group of the next. There are 20 different kinds of amino acids in proteins. Each one has a functional group (the “R group”) attached to it. Different R group ...
Honors Bio – Key concepts for final
Honors Bio – Key concepts for final

... o Isotopes  How is potential energy related to electron levels? o Electrons occupy energy levels that have a maximum occupancy o Further away from the nucleus  higher energy level.  What happens when an electron moves from one level to another? o Electrons absorb and release energy all the time o ...
Ch 8 Chapter Summary
Ch 8 Chapter Summary

... Although organisms use ATP continuously, ATP is a renewable resource that can be regenerated by the addition of a phosphate group to ADP. The free energy to phosphorylate ADP comes from exergonic (catabolic) reactions in the cell. The ATP cycle, the shuttling of inorganic phosphate and energy, coupl ...
Enzymes and Vitamins Chapter 21 Problem
Enzymes and Vitamins Chapter 21 Problem

... b. Increasing the temperature from its optimum value decreases the rate of reaction; the optimum value is the temperature at which the enzyme exhibits maximum activity. c. Increasing the amount of enzyme (arginase) increases the rate of reaction; higher enzyme concentration allows more substrate mol ...
Chapter 8 Notes
Chapter 8 Notes

Organic Compounds
Organic Compounds

... amino group (which is basic) and an acid group. Proteins consist of long chains of amino acids, with the acid group of one bonded to the amino group of the next. ...
Amino Acid Metabolism 1. Explain the role of glutamate in amino
Amino Acid Metabolism 1. Explain the role of glutamate in amino

... 1. Glutamate dehydrogenase plays a key role in fixing ammonia into organic nitrogen. The amino group of glutamate can then be used to convert a wide variety of keto acids into the corresponding amino acid. During amino acid degradation, the amino groups of amino acids are transferred to alpha-ketogl ...
Impact of scaffold rigidity on the design and
Impact of scaffold rigidity on the design and

... has been elicited in response to immunogenic transition-state analogs (7–12). Analogous nucleic acid-based catalysts have been isolated from large random libraries with powerful in vitro selection techniques (13–16). In a different line of attack, metal ion catalysis has been combined with diverse b ...
course outline - Department of LD
course outline - Department of LD

Cellular Energetics: Thermodynamics, ATP, Cellular
Cellular Energetics: Thermodynamics, ATP, Cellular

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Genit 7

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Vitamins and Coenzymes - KSU - Home

... Iron-sulfur clusters • Iron atoms are complexed with an equal number of sulfide ions (S2-) and with thiolate groups of Cys side chains ...
BIOCHEMISTRY - Mexico Central School District
BIOCHEMISTRY - Mexico Central School District

... There are an extremely large number of different proteins in life! Protein variety comes from: • Differences in the number of amino acids in the chain • Types of amino acids in the chain • Arrangement of amino acids in the chain ...
Phytochemistry 24:
Phytochemistry 24:

... pH optima for the biosynthetic and transferase activities were 7.9 and 6.5 respectively. lug’+-activated GS was strongly inhibited by Mn” and Ca’+; Co”, while also inhibitory, allowed an alternate, more active form of GS after addition of glutamate. Activity was also inhibited by possible feedback i ...
QM/MM Study of Cytochrome P450 BM3
QM/MM Study of Cytochrome P450 BM3

... F87 plays a “gatekeeper” role in that its bulky side chain must be rotated in order to allow for substrate binding. ...
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Translation Notes

Chapter 2 The Chemistry of Life
Chapter 2 The Chemistry of Life

... sugar, base, phosphate group •DNA, deoxyribonucleic acid, 2 strands of nucleotides that spiral around each other •RNA, ribonucleic acid, single strand ...
Chapter 8 Multiple Choice Practice
Chapter 8 Multiple Choice Practice

... e. The reaction would result in products (C + D) with a greater free-energy content than in the initial reactants (A + B). ____ 19. Which of the following is likely to lead to an increase in the concentration of ATP in a cell? a. an increase in a cell's anabolic activity b. an increase in a cell's c ...
Chapter 21 - Cengage Learning
Chapter 21 - Cengage Learning

... Biochemistry, the chemistry of living systems, is a subject that concerns everyone. How do our bodies extract chemical energy from sugar and other substances? How can we find cures for diseases? The answers to these questions lie in the biochemistry of the human body. To begin to understand how the ...
91 3 • cyclic adenosine monophosphate (cAMP) • diacylglycerol
91 3 • cyclic adenosine monophosphate (cAMP) • diacylglycerol

... activates a particular type of monomeric Gprotein. There are many different monomeric signaling proteins in the cells that can bind GTP or GDP. The functions of these monomeric Gproteins differ from the functions of the heterotrimeric G-proteins. In their inactive form, the monomeric G-proteins have ...
Chapter 4: Energy and Cellular Metabolism, Part 2
Chapter 4: Energy and Cellular Metabolism, Part 2

... Ch 4: Cellular Metabolism - Part 2 ...
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Enzyme



Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.
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