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Current Opinion in Chemical Biology, 2013
Echinomycin is an antitumor antibiotic secondary metabolite isolated from streptomycetes, whose core structure is biosynthesized by nonribosomal peptide synthetase (NRPS). The echinomycin biosynthetic pathway was successfully reconstituted in Escherichia coli.
Michio, Sato +4 more
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Echinomycin is an antitumor antibiotic secondary metabolite isolated from streptomycetes, whose core structure is biosynthesized by nonribosomal peptide synthetase (NRPS). The echinomycin biosynthetic pathway was successfully reconstituted in Escherichia coli.
Michio, Sato +4 more
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Biosynthesis of versicolorin A
Applied and Environmental Microbiology, 1980The incorporation of various potential intermediates into versicolorin A by a versicolorin A-accumulating mutant of Aspergillus parasiticus was studied. Both whole mycelium and cell-free extracts of this mutant were able to convert 14C-labeled versiconal hemiacetal acetate to versicolorin A.
M S, Anderson, M F, Dutton
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The biosynthesis of isopimpinellin
Canadian Journal of Biochemistry, 1977Bergapten and xanthotoxin, labelled in the methyl group with carbon-14 or tritiated at three skeletal carbons, were administered to leaves of Heracleum lanatum and to cell cultures of Ruta graveolens. In all experiments xanthotoxin was the more efficient precursor of isopimpinellin, although bergapten was always incorporated to a measurable extent ...
S A, Brown, S, Sampathkumar
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Canadian Journal of Biochemistry, 1968
A Streptomyces species (PRL 1642) was grown on media containing compounds labeled with 14C or 15N. Valinomycin was isolated from the cultures and degraded to show the distribution of the isotopes. D-α-Hydroxyisovaleric-1-14C acid was incorporated specifically into the D-α-hydroxyisovaleryl portion of valinomycin, and the L-isomer was not incorporated.
J C, MacDonald, G P, Slater
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A Streptomyces species (PRL 1642) was grown on media containing compounds labeled with 14C or 15N. Valinomycin was isolated from the cultures and degraded to show the distribution of the isotopes. D-α-Hydroxyisovaleric-1-14C acid was incorporated specifically into the D-α-hydroxyisovaleryl portion of valinomycin, and the L-isomer was not incorporated.
J C, MacDonald, G P, Slater
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EcoSal Plus, 2007
Proline was among the last biosynthetic precursors to have its biosynthetic pathway unraveled. This review recapitulates the findings on the biosynthesis and transport of proline. Glutamyl kinase (GK) catalyzes the ATP-dependent phosphorylation of L-glutamic acid.
Laszlo N, Csonka, Thomas, Leisinger
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Proline was among the last biosynthetic precursors to have its biosynthetic pathway unraveled. This review recapitulates the findings on the biosynthesis and transport of proline. Glutamyl kinase (GK) catalyzes the ATP-dependent phosphorylation of L-glutamic acid.
Laszlo N, Csonka, Thomas, Leisinger
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1976
Publisher Summary This chapter emphasizes the potential applications of studies of complement biosynthesis and presents a review of the historical aspects of work on this problem. The methods for studies of complement synthesis include tissue culture conditions (media and cells), assay systems, biosynthesis in vivo, and a criteria for establishing ...
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Publisher Summary This chapter emphasizes the potential applications of studies of complement biosynthesis and presents a review of the historical aspects of work on this problem. The methods for studies of complement synthesis include tissue culture conditions (media and cells), assay systems, biosynthesis in vivo, and a criteria for establishing ...
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Biosynthesis of selenophosphate
BioFactors, 1999AbstractSelenophosphate synthetase, the product of the selD gene, produces the highly active selenium donor, monoselenophosphate, from selenide and ATP. Positional isotope exchange experiments have shown hydrolysis of ATP occurs by way of a phosphoryl‐enzyme intermediate.
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The Biosynthesis of Deoxyribonucleotides
2004Ribonucleotide reductases play a central role in DNA biosynthesis. They catalyze the conversion of NDPs (NTPs) to dNDPs (dNTPs) concomitant with oxidation of thiols within their active sites. A single active site can accomodate reduction of both purine and pyrimidine nucleotides.
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