Q: How is methionine synthesized?
A: methionine [M] is one of the 20 amino acids that any organism requires for life processes. it is a…
Q: Why must cholesterol be transported through the bloodstream in lipoprotein particles?
A: Proteins are known to be extremely complex macromolecular components. They are located in all living…
Q: What is tetrodotoxin?
A: Toxic is a substance that causes harmful effects in humans as well as other organisms. Toxicity is a…
Q: What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.
A: Introduction: Enzymes are the catalyst of life. Enzyme inhibitor is defined as a substance which…
Q: What is Eman?
A: EMAN is a software package tool for analyzing the performance of semiautomated single-particle…
Q: Why does trypsin inhibitor exist?
A: Trypsin is an enzyme secreted in the small intestine to continue the process of protein digestion…
Q: Why is B-D-Glucopyranose in a chair conformation form is the most stable form of glucose present in…
A: B-D-Glucopyranose is a form of D-glucose which is a hexose monosaccharide unit that consists of six…
Q: What is deoxyribonucleic acid ?
A: The molecules that are found in the living cells are called biomolecules. The four main biomolecules…
Q: Substituting (changing) a purine to a purine is called:
A: A mutation is a change in a DNA sequence. It can result from DNA copying mistakes made during cell…
Q: What Is gamma-crystallin?
A: Gamma-crystallin is a type of protein. A protein is a type of biomolecule consisting of either one…
Q: H,N NH, NH H;N он
A: Trypsin is a serine protease that cleaves the carboxyl-terminal of arginine /lysine and the amino…
Q: What is the purpose of treating a sickle-cell patient with hydroxyurea?
A: Sickle cell anemia is a form of anemia in which a mutated form of hemoglobin distorts the red blood…
Q: The amino acids glutamine and glutamate are central toamino acid metabolism. Explain.
A: The metabolism of amino acids plays a vital role in our body to aid various biological reactions.…
Q: Figure 2 shows the structure of Diidopropylphosphofluoridate. Explain how this compound inhibits…
A: Enzymes are those molecules that increase the pace of the reaction without undergoing any change to…
Q: Define the term GABA (gamma-aminobutyric acid)?
A: GABA (Gamma Aminobutyric Acid ) is a natural occurring amino acid that work as a neurotransmitter in…
Q: Lesch nyhan syndrome is due to deficiency of which enzyme ?
A: Lesch nyhan syndrome is a rare inherited disorder which occurs exclusively in males, due to…
Q: The two reactions that convert glutamate to ornithine are, first, a of the y-carboxylate group of…
A: Ornithine is a proteogenic amino acid that plays a role in the urea cycle. It is mainly formed from…
Q: Why is D-glucose (dextrose), given intravenously to patients rather than sucrose?
A: In case of weakness sugar molecules are given intravenously and sometimes drugs are also dissolved…
Q: What special properties of transition metals make them especially useful in enzyme catalysis?
A: Transition metals are metals that are present between group 2 and group 13 in the periodic table.…
Q: D-Erythrulose in cyclic form:
A: Erythrulose is chemically teterose carbohydrates.formula for erythrulose is C4H8O4. It is used in…
Q: Why does the body convert NH4 + to urea for excretion?
A: Ammonia is waste product made by the body during the digestion of protein.
Q: Why "cellulose is composed of a long, branced chain of B-glucose subunits" is false?
A: Introduction Polysaccharides, also known as polycarbohydrates, are the most common type of…
Q: Why must cholesterol be packaged for transport rather than occurring freely in the bloodstream?
A: Cholesterol is a class of derived lipids made up of fused cyclohexane and cyclopentane rings which…
Q: How are lipid molecules such as estrogen and β-carotene related to each other? What biosynthetic…
A: The lipid molecule such as estrogen and b- carotene are both derived from the biosynthetic pathway…
Q: Can an amino acid be both glucogenic and ketogenic? Explain why or why not.
A: The the amino acid is the basic subunit of the protein, which helps to form protein functional…
Q: Treatment of isovaleric aciduria : a. Arginine b. Lysine c. Glycine d. Methionine
A: Isovaleric aciduria occur due to defective catabolism of leucine due to deficiency of enzymes…
Q: What type of interactions can glutamic acid participate in that are not possible for glutamine?…
A: In a biochemical context, the amino acids glutamine and glutamic acid are strongly connected.…
Q: If thymine nucleotides are degraded by the same enzymes as those catabolizing uridine nucleotides,…
A: The cleavage of the ring structures metabolizes thymine and uracil nucleotides. The usual end…
Q: what is purine ?
A:
Q: What is the medical diagnostic value associated with the presence of the following enzyme in the…
A: Enzymes act as biological catalysts and it is a protein. The chemical reactions are accelerated by…
Q: although one or more carbon atoms of glutamate can be incorporated into most carbon-containing…
A: Organisms contain four major atoms. These are carbon, hydrogen, oxygen, and nitrogen. The four major…
Q: Why do we say. Blood Urea, not Serium Urea..... Likewise, why do we say... Serium Kiriatinine and…
A: The nitrogenous end products of metabolism are urea and creatinine. Urea is the major metabolite…
Q: Tyrosine is a nonessential amino acid in humans. Under what circumstance would it become an…
A: Amino acids are biomolecules serving as the building blocks of proteins. These have a carboxylic…
Q: Why is lipid metabolism also known as a β-oxidation reaction?
A: It is asked why is lipid metabolism also known as a β-oxidation reaction?
Q: What is the cAMP phosphodiesterase?
A: Biological macromolecules are those large molecules that are necessary for the survival and growth…
Q: What would be the characteristics of a transition-state analog for the chymotrypsin reaction?
A: Introduction: Enzymes are proteins that act as a catalyst which means they increase the rate of…
Q: This is a conjectural question: If the reactive part of coenzyme A is the thioester, why is the…
A: Coenzyme A Is an important coenzyme that plays an important role in many metabolic pathways.the…
Q: What does it mean when a person is lactose intolerant? Biologically, what causes this? How can it…
A: Lactose intolerance occurs when our bodies are unable to digest or break down lactose. Lactose is a…
Q: What is the mechanism of action of acetylcysteine
A: In persons with lung disorders such as asthma, emphysema, bronchitis, and cystic fibrosis,…
Q: What is coenzyme A and why is it important?
A: Coenzyme A is a coenzyme that contains pantothenic acid, adenosine 3-phosphate 5-pyrophosphate, and…
Q: What would be the most direct result if NAG (N-acetylglucosamine acid) could not be synthesized?
A: NAG(N-acetylglucosamine acid) - This process acts as a secondary amide in the middle of acetic acid…
Q: What would be the fate of oxaloacetate if there were sufficient fluoroacetate present?
A: The Kreb cycle begins with the condensation of an oxaloacetate, and the acetyl group of acetyl-CoA.…
Q: What is proteorhodopsin and why is it so named?
A: Bacteria are characterised by the presence of peptidoglycan wall, a compact but naked DNA with…
Q: Why is triose phosphate isomerase considered to be catalytically perfect?
A: Diffusion-limited reactions are reactions where the rate of the reaction is solely dependent upon…
Q: What do leptin deficiency and Prader–Willi syndrome have in common?
A: The Prader-Willi syndrome is the disease associated with the hypotonia, hypopigmentation, short…
Q: PKU is an abbreviation for what disorder? What are the symptoms of PKU? How can PKU be treated for a…
A: Phenylketonurina is a rare inherited disorder that causes an amino acid called phenylalanine to…
Q: What is the CAMP phosphodiesterase?
A: Carbohydrates, lipids, proteins, and nucleic acids are four important biological macromolecules with…
Q: What do carboxypeptidase andaminopeptidase have in common? Identify asmany differences between them…
A: Aminopeptidase and carboxypeptidase are the protease class of enzymes. Proteases hydrolyze the…
Why is trypsin an unusual name for an enzyme? (What is the convention for enzyme names?)
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