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Metabolic networks: enzyme function and metabolite structure
Metabolic networks: enzyme function and metabolite structure

... network, and that they had not considered the irreversibility of certain types of reactions. As a result, glucose was estimated to be two reaction steps away from pyruvate due to the connectivity of glucose to ATP, through hexokinase, which in turn is connected to ADP, which is connected to pyruvate ...
Problem Set 1 - Berkeley MCB
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... (I) Is FAD a better oxidizer than NAD+? Explain your answer using numbers in the Table. ...
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Practice Exam #2.1 - Montana State University Billings
Practice Exam #2.1 - Montana State University Billings

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Question 2. Which of the following statements about G proteins are

... Question 11. For the hydrolysis of ATP to ADP + Pi, the standard free energy change is Go’=–7.3 kcal/mol. However, inside cells the G value for the hydrolysis of ATP to ADP +Pi is approximately –12 kcal/mol. Use this information to calculate the approximate ratio of [ATP] to [ADP][Pi] found in ce ...
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... Amino acids are linked by a special covalent bond called a Peptide. The first amino acid set down in every protein is Methionine. Five important functions of my favorite organic compound are Structural, Hormones, Enzymes, Antibodies and Carrier Protein. Protein are found in 4 shapes: Primary, Second ...
Structural and enzymatic characterization of a glycoside hydrolase
Structural and enzymatic characterization of a glycoside hydrolase

... which also contains diverse enzymes active on α-glucosidic bonds, such as α-glucosidases, sucrose-isomaltases, α-glucan lyases and isomaltosyltransglucosidases. Whole-genome analysis of C. japonicus has suggested that this organism produces only a single GH31 α-xylosidase, CjXyl31A [6], which is thu ...
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Crystal Structure of the Carboxyltransferase Domain of Acetyl
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... way that the N domain of one molecule is placed next to the C domain of the other (Fig. 1C). The ␣6A-␣6D insertion in the C domain of one monomer (Fig. 2B) is interdigitated between the ␤7A-␤7D insertion (Fig. 2A) and the core of the N domain of the other monomer (Fig. 1C). The insertion between ␤4 ...
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Topic 3.2: Carbohydrates, Lipids, and Proteins
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... 2. ________________ are spliced out of the RNA by units called ___________ (small nuclear ribonuclear proteins) that form a large assembly called a ______________________. C. Following processing, the m-RNA molecule moves into the cytoplasm to a _____________________, where the polypeptide is manufa ...
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... Straining bonds in reactants to make it easier to achieve transition state  Positioning reactants together to facilitate ...
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Chemistry in Living Things - Mercer Island School District
Chemistry in Living Things - Mercer Island School District

... • There are 2 Types of Nucleic Acids: DNA and RNA • Stores hereditary information in the cell by the order of the bases A, C, T and G ...
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 ...
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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 ...
BIOLOGY 311C - Brand Spring 2009
BIOLOGY 311C - Brand Spring 2009

... a. function rapidly over a narrow range of temperatures. b. function rapidly over a broad range of pH values. c. contain an adaptable binding site so it can react with many different kinds of substrate. d. be a fibrous protein. ...
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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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