scholarly journals Reduced purine biosynthesis in humans after their divergence from Neandertals

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Vita Stepanova ◽  
Kaja Ewa Moczulska ◽  
Guido Vacano ◽  
Ilia Kurochkin ◽  
Xiangchun Ju ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
De Novo ◽  
Modern Human ◽  
The Other ◽  
Purine Biosynthesis ◽  
Adenylosuccinate Lyase ◽  
The Brain

We analyze the metabolomes of humans, chimpanzees and macaques in muscle, kidney and three different regions of the brain. Whereas several compounds in amino acid metabolism occur at either higher or lower concentrations in humans than in the other primates, metabolites downstream of adenylosuccinate lyase, which catalyzes two reactions in purine synthesis, occur at lower concentrations in humans. This enzyme carries an amino acid substitution that is present in all humans today but absent in Neandertals. By introducing the modern human substitution into the genomes of mice, as well as the ancestral, Neandertal-like substitution into the genomes of human cells, we show that this amino acid substitution contributes to much or all of the reduction of de novo synthesis of purines in humans.

scholarly journals Reduced purine biosynthesis in humans after their divergence from Neandertals

2020 ◽  
Author(s):  
Vita Stepanova ◽  
Kaja Ewa Moczulska ◽  
Guido N. Vacano ◽  
Xiang-chun Ju ◽  
Stephan Riesenberg ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
De Novo ◽  
Modern Human ◽  
The Other ◽  
Purine Biosynthesis ◽  
Adenylosuccinate Lyase ◽  
The Brain

AbstractWe analyze the metabolomes of humans, chimpanzees and macaques in muscle, kidney and three different regions of the brain. Whereas several compounds in amino acid metabolism occur at either higher or lower concentrations in humans than in the other primates, metabolites in oxidative phosphorylation and purine biosynthesis are consistently present in lower concentrations in the brains of humans. In particular, metabolites downstream of adenylosuccinate lyase, which catalyzes two reactions in purine synthesis, occur at lower concentrations in humans. This enzyme carries an amino acid substitution that is present in all humans today but absent in Neandertals. By introducing the modern human substitution into the genomes of mice, as well as the ancestral, Neandertal-like substitution into the genomes of human cells, we show that this amino acid substitution is responsible for much or all of the reduction of de novo synthesis of purines in humans.

Amino acid metabolism in Ancylostoma ceylanicum and Nippostrongylus brasiliensis

1987 ◽  
Vol 61 (1) ◽  
pp. 84-88 ◽  
Author(s):  
Govind Singh ◽  
Suman Gupta ◽  
J. C. Katiyar ◽  
V. M. L Srivastava
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
The Other ◽  
Nippostrongylus Brasiliensis ◽  
Ancylostoma Ceylanicum ◽  
Other Hand

ABSTRACTAncylostoma ceylanicum and Nippostrongylus brasiliensis decarboxylated most of the amino acids examined, but only a few at signficant rates. The former nematode in general possessed higher activites. Striking differences between the two parasites were, however, noticed regarding the metabolism of some of the amino acids. For instance, while alanine followed by asparate produced highest amounts of 14CO2in the presence of A. ceylanicum, proline exhibited maximum decarboxlation in case of N. brasiliensis. Tyrosine, on the other hand, did not libreate detectable CO2with either parasite. Likewise, although large number of amino acids underwent transmination with 2-oxoglutarate, only some of them elicited appreciable activity for any two parasites.

scholarly journals Amino acid metabolism and protein synthesis in lactating rats fed on a liquid diet

1990 ◽  
Vol 270 (1) ◽  
pp. 77-82 ◽  
Author(s):  
T Barber ◽  
J García de la Asunción ◽  
I R Puertes ◽  
J R Viña
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
High Protein ◽  
The Other ◽  
Small Intestinal Mucosa ◽  
Urea Synthesis ◽  
Carbamoyl Phosphate ◽  
Liver Size

1. Amino acid metabolism was studied in control virgin rats, lactating rats and virgin rats protein-pair-fed with the lactating rats (high-protein virgin rats). 2. Urinary excretion of nitrogen and urea was higher in lactating than in control virgin rats, and in high-protein virgin rats it was higher than in lactating rats. 3. The activities of urea-cycle enzymes (units/g) were higher in high-protein virgin than in lactating rats, except for arginase. In lactating rats the activities of carbamoyl-phosphate synthase, ornithine carbamoyltransferase and argininosuccinate synthase were lower than in control virgin rats. When the liver size is considered, the activities in lactating rats were similar to those in high-protein virgin rats, except for arginase. 4. N-Acetylglutamate content was higher in high-protein virgin rats than in the other two groups. 5. The rate of urea synthesis from precursors by isolated hepatocytes was higher in high-protein virgin rats than in the other two groups. 6. The flooding-dose method (L-[4-3H]phenylalanine) for measuring protein synthesis was used. The absolute synthesis rates of mammary gland, liver and small-intestinal mucosa were higher in lactating rats than in the other two groups, and in high-protein virgin rats than in control virgin rats 7. These results show that the increased needs for amino acids during lactation are met by hyperphagia and by a nitrogen-sparing mechanism.

Autophagy and amino acid metabolism in the brain: implications for epilepsy

Amino Acids ◽  
2014 ◽  
Vol 47 (10) ◽  
pp. 2113-2126 ◽  
Author(s):  
Eloy Bejarano ◽  
José Antonio Rodríguez-Navarro
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
The Brain

Amino Acid Metabolism in Plants. II. Transamination Reactions of Free Protein Amino Acids in Cell-Free Extracts of Cotyledons and Growing Tissues of Bushbean Seedlings (Phaseolus vulgaris L.)

1972 ◽  
Vol 50 (5) ◽  
pp. 538-542 ◽  
Author(s):  
J. C. Forest ◽  
F. Wightman
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
The Other ◽  
Amino Group ◽  
Phaseolus Vulgaris L ◽  
Keto Acids ◽  
Protein Amino Acids

The different transaminase reactions for 22 protein amino acids were investigated in extracts of cotyledons and growing tissues of 8-day-old bushbean seedlings when either α-ketoglutarate, oxaloacetate, pyruvate, or glyoxylate was used as amino group acceptor. The results indicate that both cotyledons and growing tissues exhibited a similar pattern of transaminase activities with respect to the amino acids normally required for protein synthesis. It was found that with the exception of proline, hydroxyproline, and cystine which did not appear to be transaminated, and of serine and threonine which were transaminated only when pyruvate or glyoxylate was provided as the amino group acceptor, all the other 17 amino acids were transaminated to different extents when each of the four keto acids tested was supplied as the amino group acceptor. Glutamic acid, aspartic acid, and alanine were, by far, the best amino group donors and α-ketoglutarate was generally found to be the best amino acceptor. Consideration is given to the number and substrate specificity of the aminotransferases catalyzing the reactions demonstrated in this study.

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