Download Amino Acid Metabolism, Third Edition by David A Bender(auth.) PDF

By David A Bender(auth.)

Amino Acid Metabolism, 3rd Edition covers all facets of the biochemistry and dietary biochemistry of the amino acids. beginning with an summary of nitrogen fixation and the incorporation of inorganic nitrogen into amino acids, the ebook then information different significant nitrogenous compounds in micro-organisms, crops and animals. Contents contain a dialogue of the catabolism of amino acids and different nitrogenous compounds in animals, and the microbiological reactions thinking about unencumber of nitrogen fuel again into the ambience. Mammalian (mainly human) protein and amino acid specifications are thought of intimately, and the tools which are used to figure out them. 

Chapters think about person amino acids, grouped in line with their metabolic foundation, and discussing their biosynthesis (in crops and micro-organisms for those who are nutritional necessities for human beings), significant metabolic roles (mainly in human metabolism) and catabolism (again commonly in human metabolism). there's additionally dialogue of regulatory mechanisms for these kinds of metabolic pathways, and of metabolic and genetic ailments affecting the (human) metabolism of amino acids.

Throughout the publication the emphasis is at the dietary value of amino acids, integration and keep an eye on of metabolism and metabolic and different disturbances of relevance to human biochemistry and health. 

  • Completely revised version of this complete textual content protecting all of the most recent findings in amino acid metabolism research
  • Written through an expert within the box
  • Covers new advances in  structural biology
  • Clear illustrations of all constructions and metabolic pathways
  • Full record of prompt extra studying for every bankruptcy and bibliography of papers brought up within the text

Chapter 1 Nitrogen Metabolism (pages 1–65):
Chapter 2 Nitrogen stability and Protein Turnover – Protein and Amino Acids in Human food (pages 67–104):
Chapter three The position of nutrition B6 in Amino Acid Metabolism (pages 105–128):
Chapter four Glycine, Serine and the One?Carbon Pool (pages 129–155):
Chapter five Amino Acids Synthesized from Glutamate: Glutamine, Proline, Ornithine, Citrulline and Arginine (pages 157–223):
Chapter 6 Amino Acids Synthesized from Aspartate: Lysine, Methionine (and Cysteine), Threonine and Isoleucine (pages 225–277):
Chapter 7 The Branched?Chain Amino Acids: Leucine, Isoleucine and Valine (pages 279–303):
Chapter eight Histidine (pages 305–322):
Chapter nine The fragrant Amino Acids: Phenylalanine, Tyrosine and Tryptophan (pages 323–376):

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Extra info for Amino Acid Metabolism, Third Edition

Sample text

Leghaemoglobin in legume root nodules is an oxygen-binding haem protein with considerable sequence homology with mammalian haemoglobins. It is at the surface of the Rhizobium bacteroids, and it serves to deliver oxygen as required for oxidative phosphorylation to produce the ATP required for nitrogen fixation, while also preventing irreversible damage to nitrogenase by maintaining a very low concentration of free oxygen. There are similar haemoglobin-like proteins in nitrogen-fixing non-legume root nodules.

The active secretion of uric acid in the distal renal tubule is inhibited by lactic and other acids. Conditions that are associated with persistent lactic acidosis (such as some types of glycogen storage disease) lead to impaired excretion of uric acid and the early development of gout. Premenopausally, women are less at risk of gout than are men, although this gender difference is lost after the menopause. There is evidence that oestrogens lower serum uric acid and, while some studies show increased uric acid excretion in response to oestrogen administration, others do not.

18 CHAPTER 1 NITROGEN METABOLISM Glutamate dehydrogenase has some activity towards other amino acids, including alanine. Inhibition of glutamate dehydrogenase by GTP increases its activity towards alanine (Hudson & Daniel, 1993). There is a nerve-tissue specific isoenzyme of glutamate dehydrogenase which has a lower Km for glutamate than the liver enzyme and is more sensitive to activation by ADP and leucine, but is insensitive to inhibition by GTP. It is only in tissues that catalyze gluconeogenesis that succinyl CoA synthetase in the citric acid cycle catalyzes substrate-level phosphorylation to yield GTP; in other tissues, the enzyme catalyzes phosphorylation of ADP to ATP.

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