Lactate dehydrogenase isoforms contain "H" and "M" subunits. In total, how many subunits are found in the isoforms? 3 4 6 8
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- Lactate dehydrogenase is a tetramer of MW 134000 g/mole composed of subunits which are equal in size. It is found in the cytoplasm of eukaryotic and prokaryotic cells. Describe the secondary, tertiary and quaternary structures of lactate dehydrogenase.What is alpha keto glutarate dehydrogenase complex?. explain very briefly.Why is phenylketonuria resulting from dihydropteridine reductase deficiency a more serious disorder than PKU resulting from phenylalaninehydroxylase deficiency?
- Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.Lactate dehydrogenase is exist as M (muscle type) lactate dehydrogenase and H (heart type) lactate dehydrogenase. What is the difference between the two isozymes and how they are related to the functions of the muscles and the heart?Phosphoglycerate mutase (PGM) catalyzes the interconversion of 3-phosphoglycerate (3PG) and 2-phosphoglycerate (2PG) in the glycolytic and gluconeogenic pathways. a) To what enzyme class does PGM belong? b) There are two distinct classes of PGM, one which is dependent on 2,3-bisphosphoglycerate (2,3-BPG), dPGM, and one which is not, iPGM. dPGM uses acid base chemistry and a phosphorylated histidine residue to interconvert 3PG and 2PG. The dPGM reaction proceeds with formation of 2,3-BPG as an intermediate. Propose a mechanism for the dPGM-catalyzed conversion of 3PG to 2PG that is consistent with this information. c) What is the purpose of 2,3-BPG (i.e., why does dPGM require it)?
- Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.The clinical symptoms of two forms of galactosemia—deficiency of galactokinase or of UDPglucose: galactose 1-phosphate uridylyltransferase—show radically different severity. Although both types produce gastric discomfort after milk ingestion, deficiency of the transferase also leads to liver, kidney, spleen, and brain dysfunction and eventual death. What products accumulate in the blood and tissues with each type of enzyme deficiency? Estimate the relative toxicities of these products from the above information.Fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. The mammalian enzyme is tetrameric, negatively regulated by both Fructose 2,6-bisphosphate and AMP. Propose three (3) distinct models for how these molecules regulate FBPase activity. Also, describe how the enzyme might differentiate between Fructose 1,6 bisphosphate and Fructose 2,6-bisphosphate binding to the allosteric site on the enzyme with particular emphasis on amino acids comprising the allosteric binding site(s).
- Why might the compound shown below acts as a transition state analog of phosphoenolpyruvate carboxykinase. Explain. A drawing of a normal transition state for this enzyme is needed.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?In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.