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Examination questions
Examination questions

... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
BIOCHEMISTRY I Spring 2013 (General medicine, Dental
BIOCHEMISTRY I Spring 2013 (General medicine, Dental

... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
Amino acids, introduction
Amino acids, introduction

... Cysteine Aspartic acid (Aspartate) Glutamic acid (Glutamate) Phenylalanine Glycine Histidine Isoleucine Lysine Leucine Methionine Asparagine Proline Glutamine Arginine Serine Threonine Valine Tryptophan Tyrosine ©CMBI 2001 ...
Amino Acid Metabolism (Chapter 20) Lecture 9:
Amino Acid Metabolism (Chapter 20) Lecture 9:

... Ketone bodies! ...
Macromolecules: Proteins
Macromolecules: Proteins

... catalysts. Cells contain thousands of different enzymes to control the functions of the cell. Enzymes must physically fit a specific substrate(s) to work properly. The place where a substrate fits an enzyme to be catalyzed is called the active site. Excess heat, a change in pH from neutral, etc. cha ...
Protein and Amino Acid Analysis
Protein and Amino Acid Analysis

... V val valine ...
secret codon
secret codon

Nutrients that Support Phase II Detoxification
Nutrients that Support Phase II Detoxification

... intermediates are conjugated and altered further before expulsion from the body. Six different major biochemical reactions occur in this phase, known as: Glutathione conjugation Amino acid conjugation Methylation Sulfation Acetylation Glucuronidation Each of these reactions works on specific types o ...
Chapter 17 - Amino Acid Metabolism
Chapter 17 - Amino Acid Metabolism

... Maple syrup urine disease - the disorder of the oxidative decarboxylation of -ketoacids derived from valine, isoleucine, and leucine caused by the missing or defect of branched-chain dehydrogenase. The levels of branched-chain amino acids and corresponding -ketoacids are markedly elevated in both ...


... The aim of this study was to develop a procedure based on Gompertz function to determine the efficiency of utilization of amino acid. The procedure was applied to determine the efficiency of utilization of dietary lysine, methionine+cystine and threonine by growing pullets and based on the efficienc ...
DNA & RNA - East Pennsboro High School
DNA & RNA - East Pennsboro High School

... Enzyme DNA polymerase unzips DNA Two new “complimentary” strands built ...
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REVISED Review 4 - Bonham Chemistry

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b. Ketogenic amino acids
b. Ketogenic amino acids

... -These pathways converge to form seven intermediate products: pyruvate, intermediates of the TCA cycle (oxaloacetate, α-ketoglutarate, fumarate, succinyl CoA), acetyl CoA and acetoacetyl CoA. ...
question #5
question #5

... proteins are made of amino acids and amino acids have nitrogen. Nucleic acids always contain nitrogen because nucleic acids consist of three parts, one of which is a nitrogen base. The other two parts are a sugar, which is made up of carbon, hydrogen, and oxygen, and a phosphate group, made up of ox ...
Macromolecules Power Point File
Macromolecules Power Point File

... yeilds a retinol molecule B) Retinol molecules play an important role as photoreceptors in eyes ...
Slide 1
Slide 1

... be synthesized in our body; The body lacks enzymes that can synthesize these amino acids from any precursor molecules.  Non-Essential Amino acids : Need not be present in diet because the body can take care of their synthesis when required or when these are deficient in the diet.  Semi-essential: ...
Carbohydrates
Carbohydrates

... A fat found in the blood. Most fat found in the diet and body fat is in the form of triglycerides. ...
LAB 7
LAB 7

... The models constructed represent the three dimensional shapes of the molecules. A protein is formed by the chemical bonding of many amino acid molecules. Proteins may contain as few as 50 or as many as 5000 or more amino acids. The chemical combinations of two amino acids are called a dipeptide. Th ...
Microbial Metabolism Lipids and Proteins - ASAB-NUST
Microbial Metabolism Lipids and Proteins - ASAB-NUST

... pathogenic, food spoilage, and soil microorganisms can use proteins as their source of carbon and energy. • They secrete protease enzymes that hydrolyze proteins and polypeptides to amino acids, which are transported into the cell and catabolized ...
Quiz 15
Quiz 15

... 7. Which type of interaction stabilizes the alpha helix and the beta pleated sheet structures of proteins? A) hydrophobic interactions B) nonpolar covalent bonds C) ionic bonds D) hydrogen bonds E) peptide bonds 8. A hydrophilic R-group of an amino acid in hemoglobin would NOT be attracted to: A) t ...
Topic: DISORDERS OF PROTEIN METABOLISM. GOUT
Topic: DISORDERS OF PROTEIN METABOLISM. GOUT

... 1. Disorder of tyrosine methabolism leads to: a) tyrosinosis b) alkaptonuria c) albinism d) phenylketonuria 2. The causes of positive nitrogen balance are: a) growth b) pregnancy c) fever d) burn 3. What substances are inhibitory transmitters? a) aspartate b) glutamate c) glycine d) Gamma-aminobutir ...
Bio II HName list2
Bio II HName list2

... Chapter 3- Biological Molecules Organic compounds Hydrocarbons Functional groups Monomers Polymers Alcohols Enzymes Condensation reaction Hydrolysis Carbohydrate Sugar Monosaccharides Ribose Deoxyribose Glucose Oligosaccharide Sucrose Lactose Polysaccharide Cellulose Starch Glycogen Chitin Lipids Fa ...
LYSINURIC PROTEIN INTOLERANCE
LYSINURIC PROTEIN INTOLERANCE

... 1) Avoiding hyperammonemia through a low protein diet. Supplements with citrulline will normalize the urea cycle activity as citrulline is a precursor of the ornithine and arginine amino acids. 2) Avoiding osteoporosis through the administration of calcium, vitamin D and other pharmacological ...
UNIT 4 NOTES
UNIT 4 NOTES

... d. polypeptide bonds bind amino acids together 4. Nucleic acids – polymers made up of monomers called nucleotides a. a nucleotide is made up of a sugar, phosphate group, and nitrogen containing base b. nucleic acids make up DNA and RNA, they are the instructions for making proteins ...
essential amino acid
essential amino acid

... Essential and Nonessential AAs Histidine Alanine Isoleucine Arginine * Leucine Asparagine Lysine Aspartic acid Methionine Cysteine * Phenylalanine Glutamic acid Threonine Glutamine * Tryptophan Glycine Valine Ornithine * Proline * Selenocysteine * Serine * Taurine * Tyrosine * (*) Essential only in ...
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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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