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l threonine/baltažiedis vairenis
Nuoroda įrašoma į mainų sritį
6 rezultatus
Highly selective L-threonine 3-dehydrogenase from Cupriavidus necator and its use in determination of L-threonine.
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l-Threonine level in blood plasma is a biomarker of some diseases and nitrogen imbalance in the body. The determination of l-threonine is interesting and is required for diagnosis and management of inherited metabolic disorder. This is the first report of the specific enzymatic determination of
Arabidopsis thaliana glyoxalase 2-1 is required during abiotic stress but is not essential under normal plant growth.
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The glyoxalase pathway, which consists of the two enzymes, GLYOXALASE 1 (GLX 1) (E.C.: 4.4.1.5) and 2 (E.C.3.1.2.6), has a vital role in chemical detoxification. In Arabidopsis thaliana there are at least four different isoforms of glyoxalase 2, two of which, GLX2-1 and GLX2-4 have not been
Characterization of recombinant Arabidopsis thaliana threonine synthase.
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Threonine synthase (TS) catalyses the last step in the biosynthesis of threonine, the pyridoxal 5'-phosphate dependent conversion of L-homoserine phosphate (HSerP) into L-threonine and inorganic phosphate. Recombinant Arabidopsis thaliana TS (aTS) was characterized to compare a higher plant TS with
A novel bifunctional aspartate kinase-homoserine dehydrogenase from the hyperthermophilic bacterium, Thermotoga maritima.
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The orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs; the domains line up in the order HseDH, AK, and regulatory domain. In the present
Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways.
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The enteric protozoan parasite Entamoeba histolytica is a unicellular eukaryote that possesses both phosphorylated and non-phosphorylated serine metabolic pathways. In the present study, we described enzymological and functional characterization of phosphoserine aminotransferase (PSAT) from E.
Vitamin B6 biosynthesis in higher plants.
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Vitamin B6 is an essential metabolite in all organisms. It can act as a coenzyme for numerous metabolic enzymes and has recently been shown to be a potent antioxidant. Plants and microorganisms have a de novo biosynthetic pathway for vitamin B6, but animals must obtain it from dietary sources. In
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