Amino Acid Metabolism, Third Edition - download pdf or read online
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 outline of nitrogen fixation and the incorporation of inorganic nitrogen into amino acids, the e-book 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 taken with unencumber of nitrogen gasoline again into the ambience. Mammalian (mainly human) protein and amino acid requisites are thought of intimately, and the equipment which are used to figure out them.
Chapters contemplate person amino acids, grouped in keeping with their metabolic foundation, and discussing their biosynthesis (in vegetation and micro-organisms for people that are nutritional necessities for human beings), significant metabolic roles (mainly in human metabolism) and catabolism (again customarily in human metabolism). there's additionally dialogue of regulatory mechanisms for most of these metabolic pathways, and of metabolic and genetic ailments affecting the (human) metabolism of amino acids.
Throughout the e-book the emphasis is at the dietary significance 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 accomplished textual content overlaying the entire most up-to-date findings in amino acid metabolism research
- Written via an expert within the box
- Covers new advances in structural biology
- Clear illustrations of all buildings and metabolic pathways
- Full checklist of instructed additional examining for every bankruptcy and bibliography of papers mentioned within the text
Chapter 1 Nitrogen Metabolism (pages 1–65):
Chapter 2 Nitrogen stability and Protein Turnover – Protein and Amino Acids in Human nutrients (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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Additional resources for Amino Acid Metabolism, Third Edition
In microorganisms that express both types of asparagine synthetase, growth on a nitrogen-limited medium leads to low expression of the ammoniumdependent enzyme and high expression of the glutamine-dependent enzyme. When high concentrations of ﬁxed nitrogen are available, it is mainly the ammonium-dependent enzyme that is expressed. This suggests that the ammonium-dependent enzyme functions at least in part as a means of removing excess ammonium (Reitzer & Magasanik, 1982). , 2003). In most plants, asparagine is the main form in which ﬁxed nitrogen is transported around the plant, the main form of nitrogen released in seed 22 CHAPTER 1 NITROGEN METABOLISM germination and the main nitrogen storage compound.
In yeast, the glutamate dehydrogenase pathway is similarly preferred when there is ample glucose available, and mutations in glutamate synthase have no effect on the rate of ammonium incorporation or growth. When glucose is limiting, the availability of 2-oxoglutarate falls. This favours the glutamate synthase pathway, since glutamate synthase has a three-fold higher afﬁnity for 2-oxoglutarate than does glutamate dehydrogenase (Magasanik, 2003). Glutamine synthetase activity is regulated by cumulative feedback inhibition by end products including alanine, serine, glycine, AMP, carbamoyl phosphate, CTP, glucosamine 6-phosphate, histidine and tryptophan, all of which act as competitive inhibitors at either the glutamate or the ATP substrate site.
4). De novo synthesis of purines is regulated by the activity of the ﬁrst step in the pathway, the synthesis of phosphoribosylamine from phosphoribosyl pyrophosphate and glutamine. Onward metabolism of IMP to either AMP or GMP is regulated by feedback inhibition of each of the enzymes that leads to a branch of the pathway by its end product. Adenylosuccinate synthetase is inhibited by its end product, AMP, while IMP dehydrogenase, which leads to the formation of GMP, is inhibited by GMP. 7). The ﬁnal two steps of IMP synthesis, formyltransferase and IMP cyclohydrolase, are catalyzed by a bifunctional protein.
Amino Acid Metabolism, Third Edition by David A Bender(auth.)