Connect With Learnsmart Labs Online Access For Prescott's Microbiology
11th Edition
ISBN: 9781260408997
Author: Joanne Willey
Publisher: Mcgraw-hill Higher Education (us)
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Chapter 12.5, Problem 1CC
Summary Introduction
Nitrogen is an important building block for cellular components such as amino
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Why would glutamate utilize the oxidative deamination pathway over transamination – especially if removal of NH4+ requires ATP? Would it not be favorable for the body to just use transamination?
Which of the following statements about the transamination and deamination steps of amino acid degradation is true?
(A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent.
(D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.
What is the physiological significance of the isozymic forms of lactate dehydrogenase (LDH)? Explain briefly.
Chapter 12 Solutions
Connect With Learnsmart Labs Online Access For Prescott's Microbiology
Ch. 12.1 - Prob. 1CCCh. 12.1 - Prob. 2CCCh. 12.1 - Prob. 3CCCh. 12.1 - Retrieve, Infer, Apply What is self-assembly? What...Ch. 12.3 - MICRO INQUIRY How might acetyl-CoA be used by the...Ch. 12.3 - Retrieve, Infer, Apply Briefly describe the three...Ch. 12.3 - Retrieve, Infer, Apply Which two enzymes are...Ch. 12.4 - Prob. 1MICh. 12.4 - MICROINQUIRY What is the difference between Lipid...Ch. 12.4 - Retrieve, Infer, Apply What is gluconeogenesis?...
Ch. 12.4 - Retrieve, Infer, Apply Describe the formation of...Ch. 12.4 - Retrieve, Infer, Apply Suppose a microorganism is...Ch. 12.4 - Retrieve, Infer, Apply Diagram the steps involved...Ch. 12.4 - Retrieve, Infer, Apply What would happen to a cell...Ch. 12.5 - Prob. 1MICh. 12.5 - Prob. 2MICh. 12.5 - Prob. 1CCCh. 12.5 - Prob. 2CCCh. 12.5 - Prob. 3CCCh. 12.5 - How do organisms assimilate sulfur? How does...Ch. 12.5 - Prob. 5CCCh. 12.5 - Prob. 6CCCh. 12.5 - Describe the glyoxylate cycle. How is it similar...Ch. 12.5 - Prob. 8CCCh. 12.6 - How is phosphorus assimilated? What roles do...Ch. 12.6 - Explain the difference between a purine and a...Ch. 12.6 - Outline the way in which purines and pyrimidines...Ch. 12.7 - Prob. 1CCCh. 12.7 - How are unsaturated fatty acids made?Ch. 12.7 - Briefly describe the pathways for triacylglycerol...Ch. 12.7 - Prob. 4CCCh. 12.7 - Activated carriers participate in carbohydrate,...Ch. 12 - Prob. 1RCCh. 12 - Prob. 2RCCh. 12 - Prob. 3RCCh. 12 - Prob. 4RCCh. 12 - Prob. 5RCCh. 12 - Prob. 6RCCh. 12 - Prob. 7RCCh. 12 - What would happen if a microorganism that depended...Ch. 12 - Intermediary carriers are in a limited supply:...Ch. 12 - Prob. 3AL
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- DEFINE AND DESCRIBE The functions of the pentose phosphate and Enter-Doudoroff pathway.arrow_forwardWhat are the effects of Glucose-6 Phosphate Dehydrogenase Deficiency? Explain its mechanism of action.arrow_forwardOutline the steps involved in the production of malonylCoA from acetyl-CoA.arrow_forward
- What is alpha keto glutarate dehydrogenase complex?. explain very briefly.arrow_forwardIn this transamination reaction (right), which of the following are the products X and Y? Oxaloacetate Glutamate A Alanine, a-ketoglutarate B Aspartate, a-ketoglutarate C Glutamate, alanine D Pyruvate, aspartatearrow_forwardIn own words, give 5 or more reasons why most of the clinical features of the diseases a-ketoglutarate dehydrogenase deficiency, succinate dehydrogenase deficiency, and fumarase deficiency involve muscle and nerve tissue? and explain those reasons.arrow_forward
- What type of reaction is catalyzed by isocitrate dehydrogenase and a-ketoglutarate dehydrogenase?arrow_forwardHow is hexane oxygenated during anoxic catabolism?arrow_forwardThe krebs cycle has 8 enzymes: citrate synthase, aconitase, isocitrate dehyrogenase, a-ketoglutarate dehydrogenase, succinyl –CoA synthease, succinate dehyrogenase, fumarase and malate dehyrogenase. a)Write name the cofactors required by each enzyme reaction. b)For each enzyme determine which of the following deascribes the type of reactions catalyzed: condensation (Carbon-carbon bond formation), dehydration (Loss of water), hydration (addition of water), decarboxylation (loss of CO2), oxidation-reduction; subsrate level phospohorylation; isomerization.arrow_forward
- Starting with lactate, explain how phosphoenolpyruvate is produced. Include reactions of essential enzymes such as pyruvate carboxylase, and phosphoenolpyruvate carboxykinase. Explain the sites of action of these enzymes.arrow_forwardOutline the mechanism of the conversion of a-ketoglutarate to succinylCoA catalyzed by α-ketoglutarate dehydrogenase complex. Include all products, coenzymes, and reactions in your discussion.arrow_forwardDescribe how α-ketoglutarate and oxaloacetate participate in amino acid catabolism.arrow_forward
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