How are the structures of the various COX enzymes different?
Q: How does chorismate mutase destabilize the ground state of its substrate?
A: Chorismate mutase It is an enzyme involved in shikimate pathway for the formation of phenylalanine…
Q: Which are the two Sources of Cytosolic Ca21+?
A: Cell signaling allows cells to receive and respond to the surrounding signals. This is mediated by…
Q: Is fadh2 an enzyme?
A: A cofactor is characterized by a non-protein chemical compound or metallic ion that is needed for an…
Q: What is Cohesin Complex?
A: DNA ( deoxyribonucleic acid) is the genetic material that the organism inherits from the parental…
Q: How is the pentose phosphate pathway controlled?
A: The pentose phosphate pathway is a metabolic pathway that runs parallel to glycolysis. It is also…
Q: What type of protein does FOG2 produce?
A: FOG 2 protein is coded by ZFPM 2. It is a family of transcription factors genes.
Q: What is adenylyl cyclase?
A: Enzymes are the molecules that has a major role in the normal functioning of body's vital functions.…
Q: What roles do the P and A sites serve?
A: At 50S ribosomal unit, A site and B site both are binding sites. They are the sites where…
Q: Which Factors alter the cytosolic Ca21 concentration?
A: Answer: Introduction: In contrast to extracellular fluid, cytosol consist of a high concentration of…
Q: What are some common features in amino acid biosynthesis?
A: Amino acid biosynthesis is the set of biochemical processes by which the amino acids are produced.…
Q: What is cox1 ?
A: The enzymes are the proteins that act as the catalyst which speeds up the chemical reaction without…
Q: Where is deoxyribonuclease found in the body?
A: Deoxyribonucleic acid (DNA) is the hereditary unit of life, which carries the genetic information in…
Q: In Metabolic Pathways, what are the nucleotide-containing compounds?
A: A nucleotide mainly consists of a sugar molecule that is either ribose in RNA or deoxyribose in DNA…
Q: what are Cohesin Complexes ?
A: A sequence of events occurring in a cell, which causes the cell to divide and forms two daughter…
Q: What is difference between cox1 and cox2?
A: Cyclooxygenase (COX) is also known as prostaglandin-endoperoxide synthase (PTGS). It is an enzyme…
Q: What is application of D_serine?
A: Amino acids are the building blocks of proteins where the combination of 20 different proteins helps…
Q: How Are Proteins Processed FollowingTranslation?
A: Proteins are biological polymers made of amino acids. Amino acids are comprised of carbon, hydrogen,…
Q: Which disease occurs when homogentisic acid oxidase is defective?
A: Genes contain all information of proteins forms inside the body. It contains genetic information…
Q: Explain the amino–imino forms of cytosine and adenine ?
A: Watson and Crick showed a mechanism for the spontaneous occurrence of transitions. Some of the…
Q: What are the possible phosphorylation sites in a target protein?
A: Protein phosphorylation It is defined as the process of reversible post translational modification…
Q: What does guanylyl cyclase convert GTP into?
A: The study of chemical reactions that occurs within living organisms is called biochemistry. This…
Q: Is the formation of the acyl-enzyme complex a unimolecular (SN1) or biomolecular(SN2) reaction?
A: The most significant difference between a ketone/aldehyde and a carboxylic acid derivative is that…
Q: What is the function of GLUT4?
A: Among the various homeostatic occasions kept up by the human body, the blood glucose level is a…
Q: What is the role of the cox1 protein in an organism?
A: Cellular respiration is a metabolic process that take place in the cells of organisms, which…
Q: What oxidizes fadh2?
A: The process of Oxidative phosphorylation harness energy through the electron transport chain and ATP…
Q: What is the role of ATP in amino acid activation?
A: Amino acid activation refers to the attachment of an amino acid to its transfer RNA (tRNA). This…
Q: Is amino acid activation energetically favored? Why or why not?
A: Introduction: Amino acid activation is done at the initiation step of the translation. This step is…
Q: What is a proteasome? Why is it important to the proper functioning of the ER?
A: Introduction Proteins are the essential biomolecules which plays a diverse role. Almost all…
Q: What is the purpose of having ACP as a distinct activating group for fatty-acid synthesis?
A: Acyl carrier protein (ACP) is an essential part of multienzyme complex known as fatty acid synthase…
Q: What is known as polyadenylation signal sequence ?
A: The central dogma of molecular biology briefs that DNA has instructions to synthesise proteins which…
Q: What do COX enzymes synthesise?
A: Arachidonic acid acts as the precursor of the molecules known as eicosanoids. There are two pathways…
Q: What are caspases?
A: Caspases is the abbreviation of Cysteine-aspartic proteases that belong to the protease enzymes…
Q: The Hatch–Slack pathway is an alternative name for _____________.
A: Photosynthesis is a biochemical process where light energy is converted into chemical energy in…
Q: How are allosteric enzymes controlled?
A: An enzyme is known as a substance, which behaves as a ‘catalyst component’ in living things.…
Q: What is TCA? What are the different enzymes involved in TCA? What are the important products in…
A: Cellular respiration is a series of metabolic reactions and activities that occur in organisms'…
Q: What cofactors are necessary for methyltransferases t Homocysteine Methionine o work?
A: Methyltransferases are primarily responsible for the transfer of methyl groups to other molecules.
Q: What is the structure, origin and catalytic role of Adenosine phosphates?
A: ADENOSINE TRIPHOSPHA TE (ATP) is an organic compound that provides energy for many processes in…
Q: What features distinguish enzymes that undergo allosteric control from those that obey the…
A: Enzymes are the biocatalyst molecules that increase the rate of reaction by decreasing the…
Q: How is carbamoyl-phosphate synthetase I (CPS-I) controlled?
A: Introduction: The end product of the metabolism of amino acids is urea.
Q: What is the action of deoxyribonuclease?
A: Deoxyribonucleases are one type of nuclease, a generic term for enzymes capable of hydrolyzing…
Q: What are the difference between chitosan and TiO2?
A: Difference between chitosan and Ti02 1.Chitosan is the natural linear polysaccharide derived from…
Q: What is the properties of ribonuclease enzyme and describe what reaction it catalyzes?
A: Ribozymes, or otherwise known as catalytic RNAs, were discovered around 15 years ago. They are…
Q: Why do allosteric enzymes have two types of binding sites?
A: Allosteric enzyme : It are enzymes that change their conformational ensemble upon binding of an…
Q: What function does ATP play in amino acid activation?
A: In a process catalyzed by a Tran-activating enzyme, each Tran molecule binds to a particular amino…
Q: How does fructose-2,6- bisphosphate play a role as an allosteric effector?
A: A molecule that binds to an enzyme and causes allosteric effects is known as an "allosteric…
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- 1. What are congenital disorders of glycosylation (CDGs)?Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation1. Why does a cell use deoxyribonuclease?
- 1. Describe the two ways by which the activity of an enzyme can be inhibited.1. The antibiotics puromycin and erythromycin are known inhibitors of protein synthesis. (a) Which part of the protein synthesis is affected by each antibiotic? (b) What could be the reason why one of them is more effective than the other one when they are given in the same dose?5. Why is cholesterol an important steroid?.
- 3. In studying normal and mutant forms of a particularhuman enzyme, a geneticist came across a particularly interesting mutant form of the enzyme. Thenormal enzyme is 227 amino acids long, but themutant form was 312 amino acids long. The extra85 amino acids occurred as a block in the middleof the normal sequence. The inserted amino acidsdo not correspond in any way to the normal proteinsequence. What are possible explanations forthis phenomenon? How would you distinguishamong them?6. Please describe the events that may result in a mature protein not having methionine asthe N-terminal amino acid.4. What is the role of decarboxylation in fatty acid synthesis? Describe another process discussed in this Biochemistry I course that uses decarboxylation for the same purpose.
