Results 151 to 160 of about 163,724 (193)

Abstract P1-01-15: Investigation of phosphoserine aminotransferase 1 and its role in breast cancer progression

open access: yes, 2018
Metastasis and endocrine resistance are two factors that complicate therapeutic intervention in breast cancer patients and lead to poorer overall survival.
Stephanie Metcalf   +3 more
semanticscholar   +2 more sources

Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis.

Biochimica et Biophysica Acta (BBA) - General Subjects, 2016
Phosphoserine aminotransferase (PSAT) catalyses the second reversible step of the phosphoserine biosynthetic pathway in Trichomonas vaginalis, which is crucial for the synthesis of serine and cysteine.PSAT from T. vaginalis (TvPSAT) was analysed using X-ray crystallography, enzyme kinetics, and molecular dynamics simulations.The crystal structure of ...
Rohit K. Singh   +3 more
semanticscholar   +3 more sources

Abstract PO2-24-07: Investigation into potential Estrogen Receptor (ER)-mediated regulation of Phosphoserine Aminotransferase (PSAT1)

Cancer Research
Breast cancer is one of the leading causes of death among women. Expression of different proteins, such as hormone receptors (HR), are used to classify different types of breast cancer (i.e., HR+BC or triple negative breast cancer (TNBC)).
M. Sumlut, J. Wittliff, Brian C. Clem
semanticscholar   +1 more source

Serine metabolism in legume nodules: Purification and properties of phosphoserine aminotransferase

Physiologia Plantarum, 1988
Enzymes involved in serine metabolism were compared in the plant cytosol fraction of root nodules from soybean [Glycine max (L.) Merr., cv. Amsoy] and lupin [Lupinus angustifolius L., cv. Uniharvest]. Soybean nodules are ureide exporters and have a serine requirement in the synthesis of these compounds, whereas lupin nodules are amide transporters and ...
Paul H. S. Reynolds   +2 more
openaire   +1 more source

Abstract 3563: Potential role for a phosphoserine aminotransferase 1 and pyruvate kinase M2 (PSAT1:PKM2) functional interaction in lung cancer cells

open access: yes, 2017
Cellular production of serine provides precursors for numerous anabolic reactions, particularly for proteins and nucleic acid synthesis and for one carbon metabolism, and this pathway has been demonstrated to be elevated in many different cancer types ...
R. B. Sit   +5 more
semanticscholar   +2 more sources

N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica.

International Journal of Biological Macromolecules, 2019
Phosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing serine. The crystal structure of E.
Rohit K. Singh   +4 more
semanticscholar   +1 more source

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

Archives of Insect Biochemistry and Physiology, 2019
In this study, we identified and characterized a phosphoserine aminotransferase (bmPSAT) from Bombyx mori (B. mori) that is responsible for l-serine biosynthesis.
M. Haque   +7 more
semanticscholar   +1 more source

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

Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
Two peaks of aspartate aminotransferase (AspAT) catalytic activity were observed during DEAE chromatography of a protein extract from alkalophilic B. circulans. The enzyme purified from the major peak appeared to be not aspartate but phosphoserine aminotransferase (PSAT) with a considerably high AspAT side activity.
N, Battchikova   +3 more
openaire   +2 more sources

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