Microbiology: An Evolving Science (Fourth Edition)
4th Edition
ISBN: 9780393615098
Author: John W. Foster, Joan L. Slonczewski
Publisher: W. W. Norton & Company
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 15, Problem 13RQ
Summary Introduction
To review:
The outlines of interconversions of 2-oxoglutarate, glutamate, and glutamine that provide nitrogen in amino acid biosynthesis.
Introduction:
An amino acid biosynthesis is a group of biological processes through which amino acids are produced. Not all amino acids can be synthesized inside the body, some will be produced by the food or given growth media. Out of 20 different amino acids, human beings are able to produce only 11 amino acids. Â
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Draw the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.
Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Illustrate the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.
What cofactors are involved in one-carbon transfer reactions of amino acid anabolism?
Chapter 15 Solutions
Microbiology: An Evolving Science (Fourth Edition)
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Please describe four different modes of the regulation of the pentose phosphate pathway.arrow_forwardWhich 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.arrow_forwardExplain why people with a hereditary deficiency of carnitine acyltransferase II have muscle weakness. Why are the symptoms more severe during fasting?arrow_forward
- Name two control mechanisms that play a role in glycogen biosynthesis. Give an example of each.arrow_forwardName the molecules used for gluconeogenesis. What are the sources of these molecules? Under what conditions would gluconeogenesis occur?arrow_forwardPhosphoglycerate 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)?arrow_forward
- Describe the γ-glutamyl cycle. How many ATPs are required to synthesize glutathione from oxoproline?arrow_forwardFructose 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).arrow_forwardWhat is the effect on gluconeogenesis and glycogen synthesis of (a) increasing the level of ATP, (b) decreasing the concentration of fructose-1,6- bisphosphate, and (c) increasing the concentration of fructose-6- phosphate?arrow_forward
- If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?arrow_forwardWhat are the fates of carbons from the ketogenic amino acids? And Name three degradation intermediates of tryptophan that play important biologicalroles.arrow_forwardwhat are the molecular way to diagnose Lactose intolerance disorder ? describe in detail about diagnostic phenomena of lactose intolerance and possible treatment.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning