When the enzyme is incubated with oxaloacetate, will oxaloacetate be observed?
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When the enzyme is incubated with oxaloacetate, will oxaloacetate be observed?
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- The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .What are the possivble oxidation product of catalase using H2O2 as the substrate? Explain in 1-3 sentencesAspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.
- Which one of the following statements is not correct for the transamination reaction that amino acid contributed? a.Pyridoxal phosphate has a crucial role in transamination reactions. b.Enzyme levels may be high in liver and muscle diseases. c.Transamination reactions are catalyzed by aminotransferases. d.Alanine aminotransferase catalyzed reactions can be given as an example for transamination reactions. e.Transamination reactions are irreversible.a-Keto acids other than a-ketoglutarate can accept the amino group from pyridoxamine in enzyme-catalyzed transamination reactions. What amino acids are formed when the following a-keto acids accept the amino group?O OO O Opyruvate oxaloacetateWhy does it make metabolic sense for UTP to inhibit carbamoyl phosphate synthetase II, whereas ATP activates the enzyme?
- "which of the following can be used to replenish oxaloacetate in the krebs cycle"a. aspartic acid b.glutamine c.asparagine d. glutamic acidName the following enzymes:a. enzyme responsible for the cutting of the sugar on the nonreducing ends of glycogen branches b. enzyme that is only present in the liver and kidney during glycogen utilization c. enzyme that catalyzes the transfer of a two-carbon fragment from a ketose donor to an aldose acceptor in PPPTrypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
- What is alpha keto glutarate dehydrogenase complex?. explain very briefly.One of the regulators of the TCA cycle is succinyl CoA. Discuss the rationale for this molecule to be used to regulate the TCA cycle [include chemical structures and chemical equations where appropriate]. What is an allosteric inhibitor? How does it operate? For what TCA enzymes does succinyl CoA act as an inhibitor? What is the metabolic role of succinyl CoA? So then why is this molecule a reasonable choice as an inhibitor of the TCA?can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..