scholarly journals Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) From Arabidopsis thaliana– the Enzyme Involved in the Phosphorylated Pathway of Serine Biosynthesis

2018 ◽  
Vol 9 ◽  
Author(s):  
Bartosz Sekula ◽  
Milosz Ruszkowski ◽  
Zbigniew Dauter
Keyword(s):  
Arabidopsis Thaliana ◽  
Structural Analysis ◽  
Phosphoserine Aminotransferase ◽  
Serine Biosynthesis

scholarly journals Phosphoserine Aminotransferase Deficiency: A Novel Disorder of the Serine Biosynthesis Pathway

2007 ◽  
Vol 80 (5) ◽  
pp. 931-937 ◽  
Author(s):  
Claire E. Hart ◽  
Valerie Race ◽  
Younes Achouri ◽  
Elsa Wiame ◽  
Mark Sharrard ◽  
...  
Keyword(s):  
Biosynthesis Pathway ◽  
Phosphoserine Aminotransferase ◽  
Serine Biosynthesis

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

IUBMB Life ◽  
1999 ◽  
Vol 48 (5) ◽  
pp. 525-529 ◽  
Author(s):  
Marie-Jose Basurko ◽  
Michele Marche ◽  
Monique Darriet ◽  
Andre Cassaigne
Keyword(s):  
Second Step ◽  
Phosphoserine Aminotransferase ◽  
Serine Biosynthesis

scholarly journals Structural Analysis of Arabidopsis thaliana Chromosome 3. I. Sequence Features of the Regions of 4,504,864 bp Covered by Sixty P1 and TAC Clones

DNA Research ◽  
2000 ◽  
Vol 7 (2) ◽  
pp. 131-135 ◽  
Author(s):  
S. Sato ◽  
Y. Nakamura ◽  
T. Kaneko ◽  
T. Katoh ◽  
E. Asamizu ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Structural Analysis ◽  
Chromosome 3 ◽  
Sequence Features

scholarly journals Artemether Exhibits Amoebicidal Activity against Acanthamoeba castellanii through Inhibition of the Serine Biosynthesis Pathway

2015 ◽  
Vol 59 (8) ◽  
pp. 4680-4688 ◽  
Author(s):  
Yihong Deng ◽  
Wei Ran ◽  
Suqin Man ◽  
Xueping Li ◽  
Hongjian Gao ◽  
...  
Keyword(s):  
Acanthamoeba Castellanii ◽  
Dependent Manner ◽  
Biosynthesis Pathway ◽  
Content Type ◽  
Phosphoserine Aminotransferase ◽  
Proteomic Approach ◽  
Phosphoglycerate Dehydrogenase ◽  
Serine Biosynthesis ◽  
Amoebicidal Activity

ABSTRACTAcanthamoebasp. parasites are the causative agents ofAcanthamoebakeratitis, fatal granulomatous amoebic encephalitis, and cutaneous infections. However, there are currently no effective drugs for these organisms. Here, we evaluated the activity of the antimalarial agent artemether againstAcanthamoeba castellaniitrophozoites and identified potential targets of this agent through a proteomic approach. Artemether exhibitedin vitroamoebicidal activity in a time- and dose-dependent manner and induced ultrastructural modification and cell apoptosis. The iTRAQ quantitative proteomic analysis identified 707 proteins that were differentially expressed after artemether treatment. We focused on phosphoglycerate dehydrogenase and phosphoserine aminotransferase in the serine biosynthesis pathway because of their importance to the growth and proliferation of protozoan and cancer cells. The expression of these proteins inAcanthamoebawas validated using quantitative real-time PCR and Western blotting after artemether treatment. The changes in the expression levels of phosphoserine aminotransferase were consistent with those of phosphoglycerate dehydrogenase. Therefore, the downregulation of phosphoserine aminotransferase may be due to the downregulation of phosphoglycerate dehydrogenase. Furthermore, exogenous serine might antagonize the activity of artemether againstAcanthamoebatrophozoites. These results indicate that the serine biosynthesis pathway is important to amoeba survival and that targeting these enzymes would improve the treatment ofAcanthamoebainfections. Artemether may be used as a phosphoglycerate dehydrogenase inhibitor to control or blockAcanthamoebainfections.

scholarly journals P.067 Phosphoserine aminotransferase (PSAT) deficiency: Imaging findings in a child with congenital microcephaly

2018 ◽  
Vol 45 (s2) ◽  
pp. S33-S33
Author(s):  
G Shapira Zaltsberg ◽  
H McMillan ◽  
E Miller
Keyword(s):  
Intractable Epilepsy ◽  
Mri Findings ◽  
Phosphoserine Aminotransferase ◽  
Magnetic Resonance Imaging Mri ◽  
Biochemical Testing ◽  
Congenital Microcephaly ◽  
Biallelic Mutations ◽  
Serine Biosynthesis ◽  
Torch Infections

Background: Serine deficiency disorders can result from deficiency in one of three enzymes. Deficiency of the second enzyme in the serine biosynthesis pathway, 3-phosphoserine aminotransferase (PSAT), has been reported in two siblings when the eldest was investigated for acquired microcephaly, progressive spasticity and intractable epilepsy. Methods: Our patient had neurological symptoms apparent at birth. Fetal magnetic resonance imaging (MRI) at 35 weeks gestation demonstrated microencephaly and simplification of the the gyration (anterior>posterior) which was confirmed upon subsequent post-natal MRI. Congenital microcephaly was apparent at birth. Results: PSAT deficiency was confirmed when exome sequencing identified biallelic mutations in PSAT1; c.44C>T, p.Ala15Val and; c.432delA, p.Pro144fs and biochemical testing noted low plasma serine 22 mcmol/L (normal 83-212 mcmol/L) and low CSF serine 10 mcmol/L (normal 22-61 mcmol/L). Despite oral serine and glycine supplementation at 4 months old the patient showed little neurodevelopmental progress and developed epileptic spasms at 10 months old. Serological testing for TORCH infections was negative. Conclusions: PSAT deficiency should be considered for patients with congenital microcephaly. Although further characterization of MRI findings in other patients is required, microencephaly with simplified gyral pattern could provide imaging clues for this rare metabolic disorder.

scholarly journals Identification and structural analysis of SINE elements in the Arabidopsis thaliana genome.

2001 ◽  
Vol 76 (3) ◽  
pp. 169-179 ◽  
Author(s):  
Fumiyoshi Myouga ◽  
Suguru Tsuchimoto ◽  
Kenichi Noma ◽  
Hisako Ohtsubo ◽  
Eiichi Ohtsubo
Keyword(s):  
Arabidopsis Thaliana ◽  
Structural Analysis ◽  
Arabidopsis Thaliana Genome

2-Phosphoglycerate phosphatase and serine biosynthesis in Veillonella alcalescens

1981 ◽  
Vol 27 (8) ◽  
pp. 808-814 ◽  
Author(s):  
J. J. Pestka ◽  
E. A. Delwiche
Keyword(s):  
Biosynthetic Pathway ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Ammonium Sulfate Precipitation ◽  
Ph Optimum ◽  
Phosphoserine Aminotransferase ◽  
Cell Extracts ◽  
Phosphoglycerate Dehydrogenase ◽  
Serine Biosynthesis

The constituent enzymes for the phosphorylated and nonphosphorylated serine biosynthetic pathways in Veillonella alcalescens were identified and included phosphoserine phosphatase, 3-phosphoglycerate dehydrogenase, glycerate dehydrogenase, phosphoserine aminotransferase, and serine–pyruvate aminotransferase. Cell extracts of the organism were also found to cause the specific dephosphorylation of 2-phosphoglycerate. The phosphatase was purified 39-fold by manganese chloride precipitation, ammonium sulfate precipitation, and DEAE-cellulose chromatography. Sephadex G-200 gel filtration data established an apparent molecular weight of 50 000 for the enzyme. The 2-phosphoglycerate phosphatase had a pH optimum of 5.5 and was distinct from phosphoglyceromutase. Assays conducted with the purified enzyme on a number of other phosphorylated intermediates indicated that the phosphatase was most specific for 2-phosphoglycerate. Glucerate, hydroxypyruvate, and serine inhibited the enzyme, whereas succinate stimulated activity. Veillonella 2-phosphoglycerate phosphatase is the first such enzyme to be described in a prokaryote and is probably involved in glycerate generation for the nonphosphorylated serine biosynthetic pathway.

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