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Practice Exam Spring 2008 answers
Practice Exam Spring 2008 answers

... 20). Which of the following accurately describes the measure of catalytic efficiency? a). Vmax/KM c). kcat/KM e). kcat : (c), kcat/KM. ...
chapter 23
chapter 23

... Fats and oils make up the most common group of lipids in your diet. These molecules are known as triglycerides. They are formed by condensation reactions in which three fatty acid molecules bond to one glycerol (a type of alcohol) molecule. Fats, such as butter and lard, come from animals, while oil ...
05D-Proteins2
05D-Proteins2

... Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings ...
ATP - Mhanafi123`s Blog
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... malate dehydrogenase Enzyme glyceraldehyde 3P dehydrogenase required NAD+ in function ...
Enzyme Catalysis Lab
Enzyme Catalysis Lab

... chains in or near the active site to change its shape or block it. Many well known poisons such as potassium-cyanide and curare are enzyme inhibitors that interfere with the active site of critical enzymes. The enzyme used in this lab, catalase, has four polypeptide chains, each composed of more tha ...
question Examination questions: Digestion and intermediary
question Examination questions: Digestion and intermediary

... (alternative names, active forms, examples of their use in metabolic reactions) (alternative names, active forms, examples of their use in metabolic reactions) (alternative names, active forms, examples of their use in metabolic reactions) (alternative names, active forms, examples of their use in m ...
Regulation of Glucose metabolism
Regulation of Glucose metabolism

... Kidney in prolonged fasting  In early starvation and beyond, the kidneys play an important role.  Kidney expresses the enzymes of gluconeogenesis, including glucose 6-phosphatase.  In late fasting about 50% of gluconeogenesis occurs in the kidney. ...
CHAPTER 3 THE CHEMISTRY OF LIFE Section 1: Matter and
CHAPTER 3 THE CHEMISTRY OF LIFE Section 1: Matter and

... Each enzyme has an active site, the region where the reaction takes place. The shape of the active site determines which reactants, or substrates, will bind to it. Each different enzyme acts only on specific substrates. Binding of the substrates causes the enzyme’s shape to change. This change cause ...
Hemoglobin
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... These patients have sickle cell trait with no clinical symptoms and can have normal life span. Or: Homozygotes (Hb SS): mutation occurs in both β-globin chain with apparent anemia and its symptoms 2- Hb C disease: Like HbS, Hb C is a mutant Hb in which glutamic acid in 6th position of β-chain is rep ...
Protein Synthesis Notes
Protein Synthesis Notes

...  Be able to find the amino acids represented on a codon table.  Appreciate the fact that there can be some mutations in DNA that won’t show up in protein, but some mutations will.  Know where in the cell the process of protein synthesis occurs. Roots, Prefixes and Suffixes I will be able to under ...
Session 11 nr. 1 - Nordic Congress in Clinical Biochemistry 2016
Session 11 nr. 1 - Nordic Congress in Clinical Biochemistry 2016

... The gut hormone, cholecystokinin (CCK), was discovered in 1928 as a gallbladder contractor. In 1968 the structure was identified as a 33 amino acid peptide with a C-terminal “active site” sequence that revealed close homology with that of gastrin. Later the CCK gene has been shown to be expressed at ...
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... receptors initiate changes in intracellular Ca2+ concentration that modulate prostaglandin signaling (PGE2 in this example) via regulation of cPLA2 and COX-2. The respective contributions to these pathways by the spatially distinct synaptic and extrasynaptic NMDA receptors have not been defined. For ...
Relationship between the structure and function of proteins
Relationship between the structure and function of proteins

... that contains 153 amino acid residues . It contains a heme group (which is a prosthetic group consisting of a protoporphyrin organic ring and a central iron atom). It is the heme group which is responsible for the oxygen binding capacity of Myoglobin. Myoglobin is very similar to Hemoglobin in both ...
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... The enzyme RuBisCO (short for ribulose biphosphate carboxylase-oxygenase) is the most abundant enzyme on earth, as it makes approximately 50% of leaf protein. It is of upmost importance to life. Although you can see that the Calvin cycle uses RuBisCO to combine a molecule of RuBP and carbon dioxide, ...
Proteins – Essential Biomolecules
Proteins – Essential Biomolecules

Mid Term Solutions - Department of Chemistry ::: CALTECH
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... Problem 9: Chaperonins: GroEL/ES (20 points) a) (4 points) Reconcile these seemingly contradictory statements: a protein’s structure is determined only by its amino acid sequence AND chaperonins are necessary for some proteins to fold correctly. Please limit your answer to a maximum of 4 sentences. ...
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... C) Humans do not have enzymes that can hydrolyze the α glycosidic linkages of cellulose. D) Humans do not have cellulose-digesting bacteria in their digestive tract. E) The digestion of cellulose is actually possible for humans. 6. An imbalanced microbiome has been associated with which of the follo ...
Metabolism Part II: The tricarboxylic acid (TCA), citric acid, or Krebs
Metabolism Part II: The tricarboxylic acid (TCA), citric acid, or Krebs

... There are several points on the TCA cycle where key intermediates are removed to provide the building blocks for the hiosynthesis of carbohydrates, proteins, lipids, nucleic acids, and specialized molecules such as chlorophyll. Oxaloacetate and a-ketoglutarate, for example, are starting materials fo ...
Regulation of the Escherichia coli Tryptophan Operon by Early
Regulation of the Escherichia coli Tryptophan Operon by Early

... 3-methylanthranilic acid (3MA) and 7-methylindole, cause derepression of the trp operon through feedback inhibition of anthranilate synthetase. Tyrosine reverses 3MA or 7-methylindole derepression, apparently by increasing the amount of chorismic acid available to the tryptophan pathway. A mutant is ...
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Amino acid sequence of PR-39

... cecropin PI with activity against Escherichia coli and several other Gram-negative bacteria. The isolation involved a number of batch-wise steps followed by several chromatography steps. The continued investigation of these antibacterial peptides has now yielded another antibacterial peptide with hi ...
Citric Acid Cycle - University of California, Berkeley
Citric Acid Cycle - University of California, Berkeley

... electrons to an electron carrier, NAD+, via a tightly bound intermediary electron carrier, FAD. Dihydroxylipoyllysine + NAD+  Lipoyllysine + NADH FAD. The flavin group is the business end of FAD; it is not linked to ribose, but to ribitol—a reduced product of ribose. Then, it is linked to a pyropho ...
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1. Sucrose is a disaccharide. The diagram shows the structure of a

... Although different proteins have different shapes, they share a number of structural features. They are formed from 20 different types of amino acid, each containing the same four chemical elements. Unlike triglycerides, proteins are polymers. Their chains are linear and never branched. The primary ...
Ch. 5: Energy and Enzymes
Ch. 5: Energy and Enzymes

... • Binding of an inhibitor (noncompetitive) to the allosteric site stabilizes inactive shape ...
Regulation of Glycolysis
Regulation of Glycolysis

... Regulation of Glycolysis January 27, 2003 Bryant Miles Because the principle function of glycolysis is to produce ATP, it must be regulated so that ATP is generated only when needed. The enzyme which controls the flux of metabolites through the glycolytic pathway is phosphofructokinase (PFK-1). PFK- ...
Archaea
Archaea

... hypothesized currently, which are not exclusive. One is that protons are generated on the outside of the membrane in step 5, which would build the proton motive force, in turn allowing ATP synthesis via ATP synthase. The other is that step four drives uptake of Na+ ions, and releasing those back acr ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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