The Biosynthesis of d-Apiose in Lemna minor

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The biosynthesis of D-apiose in Lemna minor.

Lemna minor incorporates radioactivity from n-glucose-l14C, D-glucose-2-*4C, D-glucose-3 ,4-r4c, D-glucose-6-14C, sodium acetate-Z-14C, DL-serine-3-14C, and L-methionine-14CH8 into the n-apiose moiety of cell wall polysaccharide. The mechanism of biosynthesis of this hydroxymethyltetrose was studied by determining the distribution of 14C in n-apiose after feeding various labeled precursors. Lab...

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The biosynthesis of the branched-chain sugar d-apiose in plants: functional cloning and characterization of a UDP-d-apiose/UDP-d-xylose synthase from Arabidopsis.

d-Apiose is a plant-specific branched-chain monosaccharide found in rhamnogalacturonan II (RG-II), apiogalacturonan, and several apioglycosides. Within RG-II, d-apiose serves as the binding site for borate, which leads to the formation of cross-links within the wall. Biochemical studies in duckweed and parsley have established that uridine 5'-diphospho-d-apiose (UDP-d-apiose) is formed from UDP...

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The Turnover of Nucleic Acids in Lemna minor.

A method is described for measuring the rate constants of both synthesis and degradation of nucleic acids in sterile growing cultures of Lemna minor which avoids the difficulties of environmental changes in isotope uptake and precursor pool size. In fast growing cultures the half-life of ribosomal RNA has been estimated to be between 5 and 8 days.This half-life has been shown to consist of two ...

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The Phosphorylation of Ribosomal Protein in Lemna minor.

Sterile cultures of Lemna minor have been labeled with (32)P(1), and the ribosomal proteins have been examined for radioactivity. In relatively short term labeling a radioactive protein was found which ran as a single component in both urea/acetic acid and sodium lauryl sulfate gel electrophoresis. Acid hydrolysis of the labeled protein permitted the isolation of serine phosphate. After labelin...

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D-apiose reductase from Aerobacter aerogenes.

A strain of Aerobacter aerogenes PRL-R3 has been isolated which utilizes d-apiose as its sole source of carbon. A new enzyme, d-apiose reductase, was discovered in this strain. The enzyme was not present when the strain was grown on d-glucose. d-Apiose reductase catalyzes the nicotinamide adenine dinucleotide-dependent interconversion of d-apiose and d-apiitol. The enzyme is specific for d-apio...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1967

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)96138-7