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

By David A Bender(auth.)

Amino Acid Metabolism, 3rd Edition covers all points of the biochemistry and dietary biochemistry of the amino acids. beginning with an outline of nitrogen fixation and the incorporation of inorganic nitrogen into amino acids, the booklet then info different significant nitrogenous compounds in micro-organisms, vegetation and animals. Contents comprise a dialogue of the catabolism of amino acids and different nitrogenous compounds in animals, and the microbiological reactions excited about unencumber of nitrogen gasoline again into the ambience. Mammalian (mainly human) protein and amino acid standards are thought of intimately, and the equipment which are used to figure out them. 

Chapters contemplate person amino acids, grouped based on their metabolic foundation, and discussing their biosynthesis (in crops and micro-organisms for people that are nutritional necessities for human beings), significant metabolic roles (mainly in human metabolism) and catabolism (again as a rule 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 ebook 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 variation of this complete textual content masking all of the most up-to-date findings in amino acid metabolism research
  • Written by means of an expert within the box
  • Covers new advances in  structural biology
  • Clear illustrations of all buildings and metabolic pathways
  • Full checklist of steered extra interpreting for every bankruptcy and bibliography of papers pointed out within the text

Content:
Chapter 1 Nitrogen Metabolism (pages 1–65):
Chapter 2 Nitrogen stability and Protein Turnover – Protein and Amino Acids in Human foodstuff (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 resources for Amino Acid Metabolism, Third Edition

Example text

Heterotrophic ammonia-oxidizing microorganisms metabolize organic carbon compounds and also oxidize ammonia to nitrite. A variety of nitrite-oxidizing microorganisms oxidize nitrite to nitrate (NO3−), which is then a substrate for denitrification. Many microorganisms and fungi use nitrate and nitrite as terminal electron acceptors, forming nitric oxide, nitrous oxide and then nitrogen: NO3 – → NO2 – → NO → N 2 O → N 2 These organisms flourish in anaerobic environments, especially where the concentrations of nitrate and organic carbon are relatively high (Stein & Yung, 2003).

In a strain capable of growth on glutamate as the sole carbon source, glutamate dehydrogenase synthesis is repressed and the glutamate is catabolized by transamination with oxaloacetate, yielding 2-oxoglutarate and aspartate. 10. Growth on a glutamate-rich medium induces synthesis of aspartase. This pathway also occurs in other microorganisms, but not in mammals, which lack aspartase. , 1965). 1). As well as being a substrate, aspartate also activates the enzyme by binding to a separate regulator site together with a divalent metal ion.

The reaction involves reduction of MoVI to MoIV by transfer of electrons from the substrate, followed by electron transfer to the flavin via the iron-sulphur centres and reduction of oxygen to hydrogen peroxide. Xanthine oxidase can be converted to xanthine dehydrogenase, which reduces NAD+ rather than 32 CHAPTER 1 NITROGEN METABOLISM oxygen, by formation of disulphide bridges catalyzed by glutathionedependent thiol disulphide oxidoreductase. Xanthine dehydrogenase can be converted back to the oxidase by reduction of the disulphide bridges.

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