Phosphoserine Aminotransferase, the Second Step‐Catalyzing Enzyme for Serine Biosynthesis

Basurko, Marie-Jose; Marche, Michèle; Darriet, M.; Cassaigne, André

doi:10.1080/713803557

Cited by 39 publications

(17 citation statements)

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“…Our result showed that a temperature of 25°C was suitable for expression of bmPSAT activity. Under the optimum condition, we found that the K m (6.0 mM) for PHP showed lower affinity than that of B. circulans (0.1 mM at pH 7.0; Kapetaniou, Thanassoulas, Dubnovitsky, Nounesis, & Papageorgiou, ) The K m value of bmPSAT toward glutamate (1.9 mM) was similar to that from bovine serum (1.2 mM), sheep brain (0.7 mM), E. histolytica (0.78 mM), and B. circulans (1.0 mM; Ali & Nozaki, ; Baek et al, ; Basurko, Marche, Darriet, & Cassaigne, ; Hirsch & Greenberg, ) but was lower than that from A. thaliana (5.05 mM; Ali & Nozaki, ). These results suggested that bmPSAT may be able to recognize PHP and glutamate as substrates and NADPH as a cofactor.…”

Section: Discussionmentioning

confidence: 73%

Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l‐serine synthesis from silkworm, Bombyx mori

Haque

Hirowatari

Koyanagi

et al. 2019

Arch Insect Biochem Physiol

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In this study, we identified and characterized a phosphoserine aminotransferase (bmPSAT) from Bombyx mori (B. mori) that is responsible for L-serine biosynthesis. A complementary DNA that encodes bmPSAT was cloned by reverse transcriptase polymerase reaction and sequenced. The presumed amino acid sequence revealed 47-87% identity with known PSATs from insects, humans, plants, and bacteria. Through phylogenetic analysis, we found that bmPSAT is evolutionary related to insect PSATs. Recombinant bmPSAT was produced in Escherichia coli by using a cold-shock promotor and purified to homogeneity. This enzyme utilizes phosphohydroxypyruvate and glutamate for transamination. bmPSAT messenger RNA (mRNA) was expressed at higher levels in several tissues of standard strain silkworm including the silk gland, whereas a sericindeficient silkworm strain exhibited a diminished expression of bmPSAT mRNA in the silk gland. These findings indicate that bmPSAT may play an important role in synthesizing and supplying L-serine in the larva of B. mori. K E Y W O R D S Bombyx mori, phosphoserine aminotransferase, serine, silkworm Arch. Insect Biochem. Physiol. 2019;101:e21553.wileyonlinelibrary.com/journal/arch

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Section: Discussionmentioning

confidence: 73%

Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l‐serine synthesis from silkworm, Bombyx mori

Haque

Hirowatari

Koyanagi

et al. 2019

Arch Insect Biochem Physiol

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“…4b). We observed the steepest slope for the SNP in the amino acid biosynthesis gene PSAT1 (2.7 ΔP/km; [73]), which was over three times steeper than the slope for any other SNP. Steep slopes represent a rapid change in allele frequency and suggest relatively strong selection.…”

Section: Resultsmentioning

confidence: 99%

Evidence for adaptive introgression of exons across a hybrid swarm in deer

et al. 2019

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BackgroundSecondary contact between closely related lineages can result in a variety of outcomes, including hybridization, depending upon the strength of reproductive barriers. By examining the extent to which different parts of the genome introgress, it is possible to infer the strength of selection and gain insight into the evolutionary trajectory of lineages. Following secondary contact approximately 8000 years ago in the Pacific Northwest, mule deer (Odocoileus hemionus hemionus) and black-tailed deer (O. h. columbianus) formed a hybrid swarm along the Cascade mountain range despite substantial differences in body size (up to two times) and habitat preference. In this study, we examined genetic population structure, extent of introgression, and selection pressures in freely interbreeding populations of mule deer and black-tailed deer using mitochondrial DNA sequences, 9 microsatellite loci, and 95 SNPs from protein-coding genes.ResultsWe observed bi-directional hybridization and classified approximately one third of the 172 individuals as hybrids, almost all of which were beyond the F1 generation. High genetic differentiation between black-tailed deer and mule deer at protein-coding genes suggests that there is positive divergent selection, though selection on these loci is relatively weak. Contrary to predictions, there was not greater selection on protein-coding genes thought to be associated with immune function and mate choice. Geographic cline analyses were consistent across genetic markers, suggesting long-term stability (over hundreds of generations), and indicated that the center of the hybrid swarm is 20-30 km to the east of the Cascades ridgeline, where there is a steep ecological transition from wet, forested habitat to dry, scrub habitat.ConclusionsOur data are consistent with a genetic boundary between mule deer and black-tailed deer that is porous but maintained by many loci under weak selection having a substantial cumulative effect. The absence of clear reproductive barriers and the consistent centering of geographic clines at a sharp ecotone suggests that ecology is a driver of hybrid swarm dynamics. Adaptive introgression in this study (and others) promotes gene flow and provides valuable insight into selection strength on specific genes and the evolutionary trajectory of hybridizing taxa.Electronic supplementary materialThe online version of this article (10.1186/s12862-019-1497-x) contains supplementary material, which is available to authorized users.

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“…The organic layer was evaporated and purified by silica gel chromatography (Cyclohexane/EtOAc: 8/2) to give the title compound as a white solid (0.59 mmol, 0.13 g, 52%). 1-Morpholino-2-phenylethan-1-one (28). To a solution of 2-phenylacetic-acid (0.50 g, 3.70 mmol, 1 equiv.)…”

Section: Synthesis Of Compounds 22-39mentioning

confidence: 99%

Structure–Activity Relationships (SARs) of α-Ketothioamides as Inhibitors of Phosphoglycerate Dehydrogenase (PHGDH)

et al. 2020

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For many years now, targeting deregulation within cancer cells’ metabolism has appeared as a promising strategy for the development of more specific and efficient cancer treatments. Recently, numerous reports highlighted the crucial role of the serine synthetic pathway, and particularly of the phosphoglycerate dehydrogenase (PHGDH), the first enzyme of the pathway, to sustain cancer progression. Yet, because of very weak potencies usually in cell-based settings, the inhibitors reported so far failed to lay ground on the potential of this approach. In this paper, we report a structure–activity relationship study of a series of α-ketothioamides that we have recently identified. Interestingly, this study led to a deeper understanding of the structure–activity relationship (SAR) in this series and to the identification of new PHGDH inhibitors. The activity of the more potent compounds was confirmed by cellular thermal shift assays and in cell-based experiments. We hope that this research will eventually provide a new entry point, based on this promising chemical scaffold, for the development of therapeutic agents targeting PHGDH.

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Phosphoserine Aminotransferase, the Second Step‐Catalyzing Enzyme for Serine Biosynthesis

Cited by 39 publications

References 0 publications

Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l‐serine synthesis from silkworm, Bombyx mori

Molecular characterization and expression analysis of a phosphoserine aminotransferase involving l‐serine synthesis from silkworm, Bombyx mori

Evidence for adaptive introgression of exons across a hybrid swarm in deer

Structure–Activity Relationships (SARs) of α-Ketothioamides as Inhibitors of Phosphoglycerate Dehydrogenase (PHGDH)

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