Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 25, Problem 16P
A Deficiency on 3-Phosphogtycerate Dehydrogenase Can Affect Amino Acid
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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.
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.
Chapter 25 Solutions
Biochemistry
Ch. 25 - Prob. 1PCh. 25 - Prob. 2PCh. 25 - Regulation of Glutamine Synthetase by Covalent...Ch. 25 - The Energetic Cost of Nitrogen Excretion via the...Ch. 25 - Prob. 5PCh. 25 - Prob. 6PCh. 25 - Prob. 7PCh. 25 - Prob. 8PCh. 25 - Prob. 9PCh. 25 - Prob. 10P
Ch. 25 - Prob. 11PCh. 25 - Prob. 12PCh. 25 - Prob. 13PCh. 25 - Prob. 14PCh. 25 - Prob. 15PCh. 25 - A Deficiency on 3-Phosphogtycerate Dehydrogenase...Ch. 25 - Prob. 17PCh. 25 - Prob. 18PCh. 25 - Prob. 19PCh. 25 - Consider the synthesis and degradation of tyrosine...Ch. 25 - Prob. 21PCh. 25 - Prob. 22P
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- Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.arrow_forwardWhen the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.arrow_forwardWhat is alpha keto glutarate dehydrogenase complex?. explain very briefly.arrow_forward
- 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?arrow_forwardA number of genetic deficiencies in acyl CoA dehydrogenases have been described. This deficiency presents early in life after a period of fasting. Symptoms include vomiting, lethargy, and sometimes coma. Not only are blood levels of glucose low ( hypoglycemia), but starvation-induced ketosis is absent. Provide a biochemical explanation for these last two observations.arrow_forwardThe mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by N-acetylglutamate. Briefly describe a rationale for this effect.arrow_forward
- The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by a deacylation reaction. What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenyl ester by chymotrypsin? The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate. The rates of the acylation and deacylation reactions are equal. The rate of the acylation reaction is slower than the rate of the deacylation reaction. The rate of the acylation reaction is faster than the rate of the deacylation reaction.arrow_forwardThe enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATEarrow_forwardGlutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the adenylylation of glutamine synthetase and inhibit the deadenylylation. Why do these effects make good metabolic sense?arrow_forward
- Lactate dehydrogenase isoforms contain "H" and "M" subunits. In total, how many subunits are found in the isoforms? C 2 3 4 6 8arrow_forwardThe reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this says about the occurrence of the reaction catalyzed by malate dehydrogenase in cells explain how the reaction catalyzed by citrate synthase (−31.5 kJ⋅mol−1) influences that activity of malate dehydrogenase. In addition, explain how the activity of citrate synthase functions as a regulatory point for the citric acid cyclearrow_forwardGalactose 1-phosphate: UDP-glucose uridyltransferase (GALT) is an enzyme important for the catabolism of galactose. Patients with GALT deficiency present within days of birth with feeding difficulty, fatigue, jaundice and liver problems, and failure to thrive. In addition, a buildup of galactose and its metabolites are present in the bloodstream. GALT catalyzes the following reaction in galactose catabolism. NOTE that GALT is reversible!! Classify this enzyme and explain why you classified it in this way.arrow_forward
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