Results 151 to 160 of about 46,144 (173)
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Aspartate Aminotransferase from a Thermophilic Formate-Utilizing Methanogen, Methanobacterium thermoformicicum Strain SF-4: Relation to Serine and Phosphoserine Aminotransferases, but Not to the Aspartate Aminotransferase Family

The Journal of Biochemistry, 1994
The primary structure of the aspartate aminotransferase (AspAT) of an archaebacterium, Methanobacterium thermoformicicum strain SF-4, has been determined by cloning and sequencing of the gene for the enzyme. The gene had a consensus promoter and a ribosome binding sequence of methanogens in the 5' untranslated region, followed by an open reading frame ...
T, Tanaka   +6 more
openaire   +2 more sources

Crystallographic and Solution Studies on Phosphoserine Aminotransferase (PSAT) from E.coli

1987
Phosphoserine aminotransferase from E.coli has been crystallized in space group P212121, with one ∝2 dimeric molecule per asymmetric unit. Single crystal microspectrophotometric measurements have shown that the enzyme is catalytically active in the crystal.
J. Kallen   +4 more
openaire   +1 more source

Opal suppressor phosphoseryl-tRNA is not a substrate of phosphoserine aminotransferase.

Nucleic acids symposium series, 1987
A proposal of the role of animal opal suppressor phosphoseryl (Ps)-tRNA is that Ps-tRNA plays a role as an intermediate in the metabolic pathway from 3-phosphoglycerate to glycine. The labeled [32P]phospho[3H]seryl-tRNA was prepared and used as a substrate in the reaction of bovine brain Ps aminotransferase (EC 2.6.1.52) in the presence of alpha ...
T, Mizutani   +4 more
openaire   +1 more source

Expression, purification, crystallization and preliminary crystallographic analysis of phosphoserine aminotransferase fromBacillus alcalophilus

Acta Crystallographica Section D Biological Crystallography, 2003
Phosphoserine aminotransferase (PSAT; EC 2.6.1.52) from Bacillus alcalophilus, an obligatory alkalophile with optimum growth at pH 10.6, was overexpressed in Escherichia coli, purified and crystallized under two different conditions using the hanging-drop vapour-diffusion method.
Anatoly P, Dubnovitsky   +2 more
openaire   +2 more sources

Molecular characterization of plastidic phosphoserine aminotransferase in serine biosynthesis fromArabidopsis

The Plant Journal, 1998
Summary Serine biosynthesis in plants proceeds by two pathways; a photorespiratory pathway which is associated with photorespiration and a pathway from phosphoglycerate. A cDNA encoding plastidic phosphoserine aminotransferase (PSAT) which catalyzes the formation of phosphoserine from phosphohydroxypyruvate has been isolated from
C L, Ho   +4 more
openaire   +2 more sources

Knockdown of ERN1 disturbs the expression of phosphoserine aminotransferase 1 and related genes in glioblastoma cells

Archives of Biochemistry and Biophysics
Endoplasmic reticulum stress and synthesis of serine are essential for tumor growth, but the mechanism of their interaction is not clarified yet. The overarching goal of this work was to investigate the impact of ERN1 (endoplasmic reticulum to nucleus signaling 1) inhibition on the expression of serine synthesis genes in U87MG glioblastoma cells ...
Oleksandr H. Minchenko   +6 more
openaire   +2 more sources

Abstract 1435: Investigation of phosphoserine aminotransferase 1: Its role in breast cancer progression

Cancer Research, 2018
Abstract Metastasis and endocrine resistance are two factors that complicate therapeutic intervention in breast cancer patients and lead to poorer overall survival. Metastasis is known to be responsible for 90% of cancer related deaths, and is especially prevalent in triple negative breast cancer (TNBC); while endocrine resistance can ...
Stephanie Metcalf   +4 more
openaire   +1 more source

P17.8 Phosphoserine Aminotransferase Deficiency-The Story so Far

European Journal of Paediatric Neurology, 2011
E. Davies, M.J. Sharrard, P. Baxter
openaire   +1 more source

Molecular Structure of Phosphoserine Aminotransferase from Saccharomyces cerevisiae

International Journal of Molecular Sciences, 2023
Jeong Ho Chang
exaly  

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