By David A. Bender
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 contain a dialogue of the catabolism of amino acids and different nitrogenous compounds in animals, and the microbiological reactions fascinated with unencumber of nitrogen gasoline again into the ambience. Mammalian (mainly human) protein and amino acid necessities are thought of intimately, and the equipment which are used to figure out them.
Chapters give some thought to person amino acids, grouped in keeping with their metabolic starting place, 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 more often than not in human metabolism). there's additionally dialogue of regulatory mechanisms for a majority of these 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 regulate of metabolism and metabolic and different disturbances of relevance to human biochemistry and health.
- Completely revised version of this complete textual content protecting the entire most up-to-date 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 buildings and metabolic pathways
- Full checklist of steered additional interpreting for every bankruptcy and bibliography of papers pointed out within the text
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Extra resources for Amino Acid Metabolism
The pathways of purine and pyrimidine metabolism are highly conserved, with the same steps in prokaryotes, plants and animals, although there are some differences in regulation. , 2006). 6 Purine synthesis. 10. 7 Synthesis of AMP and GMP from IMP. 2 (glutamine-utilizing). 3 Inhibitors of nucleotide metabolism in cancer chemotherapy. methotrexate azaserine, diaza-norleucine mercaptopurine ﬂuoro-uracil adenine and cytosine arabinosides Folic acid antagonist; inhibits methylation of dUMP→TMP and two methylation reactions in purine synthesis.
They are coded for by genes on the X chromosome, and recessive genetic defects resulting in low activity impair purine (and pyrimidine) synthesis in affected males. , 2007). By contrast, there are a number of dominant genetic conditions in which the activity of PRPP synthetase is elevated. In most cases, the problem is over-expression of the gene for PRPP synthetase I, with no effect on the kinetics of the reaction. In other cases, this is the result of either an increase in the Vmax of the enzyme, with no difference in the values of Km for the substrates, or sensitivity to inhibitors, or reduced sensitivity of the enzyme to feedback inhibition by ADP and GDP, which can be considered to be end products of PRPP metabolism.
Deﬁciency of the enzyme leads to the accumulation of succinylaminoimidazole carboxamide and succinyladenosine in body ﬂuids and variable degrees of psychomotor delay, convulsions and mental retardation. The relative concentrations of these two metabolites determines the severity of the disease. , 1997). In prokaryotes, the enzymes of purine synthesis are monofunctional, apart from a bifunctional enzyme that catalyzes the reactions of AICAR formyltransferase and IMP cyclohydrolase. , 2008), consisting of: 28 CHAPTER 1 NITROGEN METABOLISM • a trifunctional enzyme that catalyzes the reactions of glycinamide ribonucleotide synthetase, GAR formyltransferase and AIR synthase; • a bifunctional enzyme that catalyzes the reactions of AIR carboxylase and SAICAR synthase; • a bifunctional enzyme that catalyzes the reactions of AICAR formyltransferase and IMP cyclohydrolase, as in prokaryotes.
Amino Acid Metabolism by David A. Bender