Most aminotransferases use which α-ketoacid as their amino group acceptor? A、α-ketoglutarate B、Pyruvate C、α-ketoglutamate D、alanine E、Oxaloacetate
Q: Draw the chemical structures resulting from the transamination of the following amino acids: a.…
A: Note: We are authorized to answer three subparts at a time since you have not mentioned which part…
Q: List the essential amino acids for a phenylketonuric adultand compare them with the requirements for…
A: Phenylketonuria (PKU) is defined as a rare genetic human condition. It causes an amino acid called…
Q: Alpha-ketoglutarate is produced in which central metabolic pathway?
A: Alpha Ketoglutarate is a 5 carbon containing compound. It has many medicinal uses. It is used to…
Q: During intensive muscle work there is a large amount of ammonia produced in the muscles. What amino…
A: Gluconeogenesis can be defined as a metabolic pathway that produces glucose using precursors that…
Q: What is the relationship between -ketoglutarate, glutamate, and glutamine in amino acid anabolism?
A: Different organisms have different capacity to synthesize amino acids. Plants can produce all the…
Q: The reaction of glutamate and NH4* to yield glutamine is catalyzed by. a) Uridylyltransferase b)…
A: Enzymes are proteins(biochemical catalysts) that play a major role in speeding up biochemical…
Q: Three amino acids that donate amine groups for the purine biosynthesis are a) Glycine, glutamine,…
A: Purines are heterocyclic aromatic compound of carbon and nitrogen and forms nucleotides that in turn…
Q: Which enzymes may catalyze the transfer of an a-amino group from an α-amino acid to an α-ketoacid?…
A: Given: To find which enzymes catalyze the transfer of an a-amino group from an α-amino acid to an…
Q: Which among the following indicates correct the three-letter abbreviation and one-letter…
A: There are twenty naturally occurring amino acids. These amino acids are conventionally represented…
Q: Match the each enzyme deficiency with their corresponding disease…
A: Different enzymes are required for synthesis of spingolipids. If these enzymes are not…
Q: Identify the following amino acid (at pH = 7.0): (COO-)–CH(NH3+)–CH2–CH2–CH2–CH2–(NH3+) glutamic…
A: Amino acids are the organic molecule composed of amino group (NH2), an acidic carboxylic group…
Q: Which of the following combination is are non-essential amino acids? A. Leucine and Isoleucine…
A: Proteins are polymers of amino acids, which suggests proteins are made from amino acids. Amino acids…
Q: How would you handle a baby with argininosuccinate synthetase deficiency? Which chemicals are…
A: Arginosuccinate synthase, also known as synthetase, is an enzyme that catalyzes the conversion of…
Q: What cofactors are involved in one-carbon transfer reactions of amino acid anabolism?
A: Introduction: Every last one of the 20 normally occurring amino acids goes through its own…
Q: how do we maintain a steady support of amino acids in the body?
A: Amino acids are the basic units of proteins and proteins are very important for our body because…
Q: What characterizes the C5 amino acids? These amino acids are converted to glutamate then deaminated…
A: Introduction: Amino acids are compounds that contain an amino group, a carboxyl group, and a side…
Q: An individual with an argininosuccinase deficiency is administered benzoate and arginine. This…
A: Argininosuccinase deficiency is a condition where the cells are devoid of an important enzyme i.e.…
Q: In transamination reactions, which of the following is not a donor amino acid–acceptor α-keto acid…
A: Transamination was the process in which amino group was removed from the amino acid and transfer…
Q: Which amino acids are both ketogenic and glucogenic? 2. Which amino acids will have its C-skeletons…
A: Amino acids are the building blocks of proteins and are composed of carbon, hydrogen, nitrogen, and…
Q: (a) What is protein turnover? Give 1-2 examples. (b) What are the main differences between…
A: There are four different levels for the proteins. These levels are: Primary structure secondary…
Q: Amino acids that degrade, yielding acetyl-CoA or acetoacetylCoA, are referred to as…
A: The strategy of amino acid degradation is to transform the carbon skeletons into major metabolic…
Q: The reaction of glutamate and NH4* to yield glutamine is catalyzed by a) Uridylyltransferase b)…
A: Glutamine and glutamate are important amino acids for the metabolism of body. Though they are not…
Q: All the following amino acids are converted to succinyl-CoA except Group of answer choices Lysine…
A: There are two types of amino acids ,glucogenic amino acids and ketogenic amino acids while…
Q: Will an amino acid be glucogenic or ketogenic if it is catabolized to the following molecules?(a)…
A: Glucogenic amino acids are the amino acids that are converted into glucose through gluconeogenesis…
Q: If phenylalanine was not an essential amino acid, would diet therapy (the elimination of…
A: Phenylalanine is an essential amino acid. Essential amino acid are those amino acids that are not…
Q: - Keto counterparts. Name the a-ketoacida-ketoacid that is formed by the transamination of each of…
A: Tranamination is a reaction in which the amino group of an amino aid is transferred to an…
Q: Why is rubisco likely to be the most abundant protein in nature?
A: Proteins are organic biomolecules that play an important role in various biological cellular…
Q: (a) What are the main differences between glucogenic and ketogenic amino acids? (b) Why do would…
A: a)ANSWER;- The principal distinction between glucogenic amino acids and ketogenic amino acids is…
Q: Does HCl in the stomach hydrolyze both the 1,4- and 1,6-glycosodic bonds?
A: A glycosidic bond is a type of covalent bond that joins a carbohydrate molecule to another group,…
Q: Explain the relationship between a-ketoglutarate, glutamate, and glutamine in amino acid anabolism?
A: Amino acid anabolism means formation of amino acid. There are total 20 amino acids known. Glutamate…
Q: what is the total number of D- and L-sugars that belong to the family of ketopentoses
A: Monosaccharides consist of polyhydroxlyalcohols and these are of two types of derivatives aledhydes…
Q: In a disease known as phenylketonuria, a person is not able to break down the particular amino acid…
A: Phenylketonuria: Phenylketonuria (also referred as “PKU”) is a unique genetic condition that causes…
Q: What is a major difference between the amino acid biosynthetic capacity of prokaryotic organisms and…
A: Prokaryotes are unicellular organisms that have simple functioning and simple structure whereas…
Q: Amino acids that degrade yielding acetyl-CoA or acetoacetyl-CoA are referred to as _____________.
A: Amino acids are the monomers for protein synthesis but amino acid degradation transforms the carbon…
Q: The chemical structure of Coenzyme A contains the following EXCEPT— a β-mercaptoethylamine…
A: The correct answer is LIPOIC ACID RESIDUE
Q: What are some of the benefits of having a high number of N-glycosylation sites for a glycoprotein?
A: Conjugated proteins, such as glycoproteins, are a form of conjugated protein. They are covalently…
Q: Which three amino acids are substrates or products of serine hydroxymethyltransferase?
A: Serine hydroxymethyltransferase (SHMT) is a member of the fold type I family of vitamin B6-dependent…
Q: List the important amino acids with their biogenic amines and their derivatives .
A: Amino acids are the building blocks of proteins . Amino acids are used as a source of energy for the…
Q: Show the complete reaction mechanism for the deamination of alanine until the amino group is…
A: The deamination of the alanine amino acid takes place with the help of the transaminase enzyme to…
Q: Which of the 20 amino acids can be synthesized directly from a common metabolic intermediate by a…
A: Transamination is a chemical reaction that transfers an amino group to a keto acid to form new amino…
Q: Which of the following amino acids is/are ketogenic? A. tyrosine and phenylalanine B.lysine and…
A: A carboxylic acid group, a side-chain distinct to each amino acid, and an amine group are the three…
Q: Branched-chain amino acids are important in metabolic processes for all of the following reasons…
A: Amino acids are generally used to make protein and poly peptide chain
Q: Discuss the absorption spectra of the 3 amino acids as given in graph 1.
A: Spectrophotometry is used to determine the concentration of any unknown sample. Ninhydrin test is…
Q: The immediate donors of the nitrogen atoms of urea are: a. Aspartate and glutamate b. Glutamate and…
A: Urea cycle is a cyclic pathway related to the synthesis of urea, one nitrogen is derived from free…
Q: If both cysteine residues on the B chain of insulin were changes to alanine residues, how…
A: Insulin is made up of two chains A chain and B chain. Both the chains are linked together by two…
Q: Which of the following amino acids contains a carboxamide side chain? A.glutamine B.alanine…
A:
Q: Explain all amin acids are absorbed in L- form while methionine as amino acid absorbed in D-form?
A: Amino acids are biomolecules that contain both amino groups and carboxylate groups (–COO−). In most…
Q: What makes transamination reactions important in amino acid biosynthesis?
A: The biological mechanisms (metabolic pathways) that create amino acids are referred to as amino acid…
Step by step
Solved in 3 steps
- Will an amino acid be glucogenic or ketogenic if it is catabolized to the following molecules?(a) Phosphoenolpyruvate(b) -Ketoglutarate (c) Succinyl-CoA(d) Acetyl-CoA(e) Oxaloacetate(f) AcetoacetateFrom which amino acid is 2-phenylethanol derived and what chemical changes take place in the conversion?What cofactor is required by all aminotransferases?
- Why are L-amino acids prevalent/common in biological systems?Name the α-ketoacid that is formed by the transamination of each of the following amino acids: (a) Alanine (d) Leucine (b) Aspartate (e) Phenylalanine (c) Glutamate (f) TyrosineIllustrate the pathways to synthesize the following aminoacids:a. glutamineb. serinec. arginined. glycinee. cysteine
