By David A. Bender
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 publication then info 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 serious about liberate of nitrogen fuel again into the ambience. Mammalian (mainly human) protein and amino acid requisites are thought of intimately, and the tools which are used to figure out them.
Chapters give some thought to person amino acids, grouped in keeping with their metabolic beginning, 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 some of these metabolic pathways, and of metabolic and genetic illnesses affecting the (human) metabolism of amino acids.
Throughout the ebook 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 complete textual content masking all of the most recent findings in amino acid metabolism research
- Written by way of an expert within the box
- Covers new advances in structural biology
- Clear illustrations of all constructions and metabolic pathways
- Full checklist of instructed additional interpreting for every bankruptcy and bibliography of papers mentioned within the text
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Additional resources for Amino Acid Metabolism
Asparagine is formed from aspartate either by amidotransfer from glutamine or by incorporation of ammonium directly, the reaction of asparagine synthetase. There are two families of asparagine synthetases: those that utilize ammonium as the nitrogen donor, linked to utilization of ATP (forming AMP and pyrophosphate); and those that utilize glutamine as the nitrogen donor. In prokaryotes, these enzymes form AMP and pyrophosphate, while in eukaryotes they form ADP and phosphate. 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.
In the kidney, part of the response to metabolic acidosis is increased expression of glutaminase and glutamate dehydrogenase (to act in the direction of oxidative deamination, producing ammonium), and of ammonium transporters, so as to increase ammonium excretion in the urine. Onward metabolism of the 2-oxoglutarate arising from glutamine catabolism produces bicarbonate to increase blood buffering capacity. , 2005; Lowry & Ross, 1980; Nissim, 1999). Both glutamate and glutamine can be used as nitrogen donors for synthesis of a variety of amino acids.
Coli can use either pathway, depending on the conditions. The glutamate synthase pathway is more ATP expensive and may account for 15 per cent of total ATP utilization. It is used in growth on an energy-rich substrate; glutamate dehydrogenase is used in growth on a substrate providing adequate ammonium but limited energy. 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.