scholarly journals Correlation between equi-partition of aminoacyl-tRNA synthetases and amino-acid biosynthesis pathways

2020 ◽  
Vol 48 (6) ◽  
pp. 3277-3285 ◽  
Author(s):  
Akio Takénaka ◽  
Dino Moras
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Biosynthesis Pathway ◽  
Amino Acid Distribution ◽  
Acid Biosynthesis ◽  
Amino Acid Synthesis ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Coevolution Theory ◽  
The Common

Abstract The partition of aminoacyl-tRNA synthetases (aaRSs) into two classes of equal size and the correlated amino acid distribution is a puzzling still unexplained observation. We propose that the time scale of the amino-acid synthesis, assumed to be proportional to the number of reaction steps (NE) involved in the biosynthesis pathway, is one of the parameters that controlled the timescale of aaRSs appearance. Because all pathways are branched at fructose-6-phosphate on the metabolic pathway, this product is defined as the common origin for the NE comparison. For each amino-acid, the NE value, counted from the origin to the final product, provides a timescale for the pathways to be established. An archeological approach based on NE reveals that aaRSs of the two classes are generated in pair along this timescale. The results support the coevolution theory for the origin of the genetic code with an earlier appearance of class II aaRSs.

scholarly journals Amino acid synthesis loss in parasitoid wasps and other hymenopterans

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Xinhai Ye ◽  
Shijiao Xiong ◽  
Ziwen Teng ◽  
Yi Yang ◽  
Jiale Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Common Ancestor ◽  
Gene Loss ◽  
Acid Synthesis ◽  
Parasitoid Wasps ◽  
Amino Acid Synthesis ◽  
The Common ◽  
Multiple Loss ◽  
Lysine Synthesis ◽  
Cotesia Chilonis

Insects utilize diverse food resources which can affect the evolution of their genomic repertoire, including leading to gene losses in different nutrient pathways. Here, we investigate gene loss in amino acid synthesis pathways, with special attention to hymenopterans and parasitoid wasps. Using comparative genomics, we find that synthesis capability for tryptophan, phenylalanine, tyrosine, and histidine was lost in holometabolous insects prior to hymenopteran divergence, while valine, leucine, and isoleucine were lost in the common ancestor of Hymenoptera. Subsequently, multiple loss events of lysine synthesis occurred independently in the Parasitoida and Aculeata. Experiments in the parasitoid Cotesia chilonis confirm that it has lost the ability to synthesize eight amino acids. Our findings provide insights into amino acid synthesis evolution, and specifically can be used to inform the design of parasitoid artificial diets for pest control.

scholarly journals Filling Gaps in Bacterial Amino Acid Biosynthesis Pathways with High-throughput Genetics

2017 ◽  
Author(s):  
Morgan N. Price ◽  
Grant M. Zane ◽  
Jennifer V. Kuehl ◽  
Ryan A. Melnyk ◽  
Judy D. Wall ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
High Throughput ◽  
Heterotrophic Bacteria ◽  
Current Knowledge ◽  
Acid Synthesis ◽  
Amino Acid Biosynthesis ◽  
Desulfovibrio Vulgaris ◽  
Acid Biosynthesis ◽  
Amino Acid Synthesis

AbstractFor many bacteria with sequenced genomes, we do not understand how they synthesize some amino acids. This makes it challenging to reconstruct their metabolism, and has led to speculation that bacteria might be cross-feeding amino acids. We studied heterotrophic bacteria from 10 different genera that grow without added amino acids even though an automated tool predicts that the bacteria have gaps in their amino acid synthesis pathways. Across these bacteria, there were 11 gaps in their amino acid biosynthesis pathways that we could not fill using current knowledge. Using genome-wide mutant fitness data, we identified novel enzymes that fill 9 of the 11 gaps and hence explain the biosynthesis of methionine, threonine, serine, or histidine by bacteria from six genera. We also found that the sulfate-reducing bacteriumDesulfovibrio vulgarissynthesizes homocysteine (which is a precursor to methionine) by using DUF39, NIL/ferredoxin, and COG2122 proteins, and that homoserine is not an intermediate in this pathway. Our results suggest that most free-living bacteria can likely make all 20 amino acids and illustrate how high-throughput genetics can uncover previously-unknown amino acid biosynthesis genes.

scholarly journals Structural Basis for the Recognition of Isoleucyl-Adenylate and an Antibiotic, Mupirocin, by Isoleucyl-tRNA Synthetase

2001 ◽  
Vol 276 (50) ◽  
pp. 47387-47393 ◽  
Author(s):  
Takashi Nakama ◽  
Osamu Nureki ◽  
Shigeyuki Yokoyama
Keyword(s):  
Amino Acid ◽  
Thermus Thermophilus ◽  
High Energy ◽  
Trna Synthetase ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Trna Synthetases ◽  
Chemical Structures ◽  
Aminoacyl Trna Synthetases ◽  
The Common

An analogue of isoleucyl-adenylate (Ile-AMS) potently inhibits the isoleucyl-tRNA synthetases (IleRSs) from the three primary kingdoms, whereas the antibiotic mupirocin inhibits only the eubacterial and archaeal IleRSs, but not the eukaryotic enzymes, and therefore is clinically used against methicillin-resistantStaphylococcus aureus. We determined the crystal structures of the IleRS from the thermophilic eubacterium,Thermus thermophilus, in complexes with Ile-AMS and mupirocin at 3.0- and 2.5-Å resolutions, respectively. A structural comparison of the IleRS·Ile-AMS complex with the adenylate complexes of other aminoacyl-tRNA synthetases revealed the common recognition mode of aminoacyl-adenylate by the class I aminoacyl-tRNA synthetases. The Ile-AMS and mupirocin, which have significantly different chemical structures, are recognized by many of the same amino acid residues of the IleRS, suggesting that the antibiotic inhibits the enzymatic activity by blocking the binding site of the high energy intermediate, Ile-AMP. In contrast, the two amino acid residues that concomitantly recognize Ile-AMS and mupirocin are different between the eubacterial/archaeal IleRSs and the eukaryotic IleRSs. Mutagenic analyses revealed that the replacement of the two residues significantly changed the sensitivity to mupirocin.

scholarly journals Petasis vs. Strecker Amino Acid Synthesis: Convergence, Divergence and Opportunities in Organic Synthesis

Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1707
Author(s):  
Wayiza Masamba
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Organic Synthesis ◽  
Acid Synthesis ◽  
Physical Sciences ◽  
Amino Acid Synthesis

α-Amino acids find widespread applications in various areas of life and physical sciences. Their syntheses are carried out by a multitude of protocols, of which Petasis and Strecker reactions have emerged as the most straightforward and most widely used. Both reactions are three-component reactions using the same starting materials, except the nucleophilic species. The differences and similarities between these two important reactions are highlighted in this review.

scholarly journals Enzymatic cascade systems for D-amino acid synthesis: progress and perspectives

2021 ◽  
Author(s):  
Anwen Fan ◽  
Jiarui Li ◽  
Yangqing Yu ◽  
Danping Zhang ◽  
Yao Nie ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Cascade Systems

Reconstitution of amino acid synthesis by combining spinach chloroplasts with other leaf organelles

1979 ◽  
Vol 18 (7) ◽  
pp. 1109-1111 ◽  
Author(s):  
Barbara Buchholz ◽  
Brigitte Reupke ◽  
Horst Bickel ◽  
Gernot Schultz
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Spinach Chloroplasts

Enzymes for amino acid synthesis by design

2021 ◽  
Vol 4 (5) ◽  
pp. 348-349
Author(s):  
Christopher K. Prier
Keyword(s):  
Amino Acid ◽  
Acid Synthesis ◽  
Amino Acid Synthesis
Sign in / Sign up

Export Citation Format

Share Document