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<i>Haemophilus influenzae</i> tryptophan biosynthesis is required for lung infection. [PDF]
Front Cell Infect MicrobiolAsensio-López J +13 more
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p73 regulates serine biosynthesis in cancer [PDF]
Oncogene, 2013 Activation of serine biosynthesis supports growth and proliferation of cancer cells. Human cancers often exhibit overexpression of phosphoglycerate dehydrogenase (PHGDH), the metabolic enzyme that catalyses the reaction that diverts serine biosynthesis from the glycolytic pathway.
Gerry Melino +2 more
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Serine biosynthesis and transport defects
Molecular Genetics and Metabolism, 2016l-serine is a non-essential amino acid that is biosynthesized via the enzymes phosphoglycerate dehydrogenase (PGDH), phosphoserine aminotransferase (PSAT), and phosphoserine phosphatase (PSP). Besides its role in protein synthesis, l-serine is a potent neurotrophic factor and a precursor of a number of essential compounds including phosphatidylserine ...
Ayman El-Hattab
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Studies on the biosynthesis of phosphatidyl serine
Biochimica et Biophysica Acta, 1959Abstract 1. 1. A method is described for the determination of the radioactivity of [ 14 C]-phospholipids using a liquid scintillation counter. 2. 2. The incorporation of l -[ 14 C]serine into mitochondrial phospholipids was studied. CMP, ATP, CoASH, glutathione, glycerophosphate and magnesium ions were required for optimal incorporation. CTP
G, HUBSCHER, R R, DILS, W F, POVER
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Serine in plants: biosynthesis, metabolism, and functions
Trends in Plant Science, 2014Serine (Ser) has a fundamental role in metabolism and signaling in living organisms. In plants, the existence of different pathways of Ser biosynthesis has complicated our understanding of this amino acid homeostasis. The photorespiratory glycolate pathway has been considered to be of major importance, whereas the nonphotorespiratory phosphorylated ...
Stephan Krueger +2 more
exaly +3 more sources
The Enzymes of Serine Biosynthesis
Journal of Experimental Botany, 1969Extracts of etiolated epicotyls of Pisum sativum have been shown to contain the enzymes necessary for the conversion of phosphohydroxypyruvate to serine. L-Glutamate acted as the amino donor in the formation of phosphoserine from phosphohydroxypyruvate while both L-alanine and L-aspartic acid were inactive.
J. C. SLAUGHTER, D. D. DAVIES
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Enzymes of serine biosynthesis in Rhodopseudomonas capsulata
Archives of Biochemistry and Biophysics, 1973Rhodopseudomonas capsulata has been shown to possess all the enzymatic activities of both the phosphorylated and nonphosphorylated pathways of serine biosynthesis. In addition there was an active serine hydroxymethyltransferase which catalyzed the reversible interconversion of serine and glycine.
L S, Schmidt, G A, Sojka
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Serine biosynthesis in Tetrahymena pyriformis S
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1971Abstract 1. 1. Glycine transhydroxymethylase and threonine aldolase function in the formation of serine in Tetrahymena pyriformis S. 2. 2. Both the phosphorylated and non-phosphorylated pathways of serine biosynthesis from 3-phosphoglycerate are also operative. 3. 3. Tricarboxylic acid cycle intermediates also serve as serine precursors
G R, Seaman, J, Cicmanec, M, Koll
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On the phenotypic spectrum of serine biosynthesis defects
Journal of Inherited Metabolic Disease, 2016AbstractL‐serine is a non‐essential amino acid that is de novo synthesized via the enzymes phosphoglycerate dehydrogenase (PGDH), phosphoserine aminotransferase (PSAT), and phosphoserine phosphatase (PSP). Besides its role in protein synthesis, L‐serine is a precursor of a number of important compounds.
Ayman W, El-Hattab +6 more
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