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Arabinose C Protein: Regulation of the Arabinose Operon in vitro
Nature New Biology, 1971The detection of the gene ara C protein using a DNA-dependent in vitro protein synthesizing system represents the first isolation of an operon specific positive regulator with an in vivo role that has been genetically defined.
J, Greenblatt, R, Schleif
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European Journal of Organic Chemistry, 2013
AbstractMetabolically stable arabinose 5‐phosphate analogues possessing phosphate mimetic groups at the 5‐position were synthesized and evaluated by saturation‐transfer‐difference (STD) NMR studies for their ability to interact with arabinose 5‐phosphate isomerase.
GABRIELLI, LUCA +6 more
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AbstractMetabolically stable arabinose 5‐phosphate analogues possessing phosphate mimetic groups at the 5‐position were synthesized and evaluated by saturation‐transfer‐difference (STD) NMR studies for their ability to interact with arabinose 5‐phosphate isomerase.
GABRIELLI, LUCA +6 more
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Journal of Agricultural and Food Chemistry, 2023
During the production of ethanol from lignocellulose-derived sugars, recombinant yeasts tend to utilize xylose and arabinose after glucose exhaustion. So far, many glucose-insensitive pentose transporters have been reported to counteract this phenomenon, but few studies have described intracellular factors.
Jinle Liu +7 more
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During the production of ethanol from lignocellulose-derived sugars, recombinant yeasts tend to utilize xylose and arabinose after glucose exhaustion. So far, many glucose-insensitive pentose transporters have been reported to counteract this phenomenon, but few studies have described intracellular factors.
Jinle Liu +7 more
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Liebigs Annalen der Chemie, 1980
AbstractAus D‐Arabinose wird über eine Wittig‐Reaktion des teilgeschützten Derivates 8 das Zwischen‐produkt 17 gewonnen, das in ( + )‐Biotin (1) übergeführt werden kann.
Friedrich G. M. Vogel +2 more
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AbstractAus D‐Arabinose wird über eine Wittig‐Reaktion des teilgeschützten Derivates 8 das Zwischen‐produkt 17 gewonnen, das in ( + )‐Biotin (1) übergeführt werden kann.
Friedrich G. M. Vogel +2 more
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An l-arabinose binding protein and arabinose permeation in Escherichia coli
Journal of Molecular Biology, 1969Abstract A search was made for proteins of the arabinose system which bind arabinose, as it is expected that the permease and possibly the C protein could be identified by arabinose binding. One protein was found and this is most probably part of the arabinose permease. It is inducible, can be removed from cells by osmotic shock and easily purified,
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Crystal structure of bacterial L-arabinose 1-dehydrogenase in complex with L-arabinose and NADP+
Biochemical and Biophysical Research Communications, 2020L-Arabinose 1-dehydrogenase (AraDH) is responsible for the first step of the non-phosphorylative L-arabinose pathway from bacteria, and catalyzes the NAD(P)+-dependent oxidation of L-arabinose to L-arabinonolactone. This enzyme belongs to the so-called Gfo/Idh/MocA protein superfamily, but has a very poor phylogenetic relationship with other functional
Kentaroh Yoshiwara +2 more
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Arabinose 5-phosphate covalently inhibits transaldolase
Journal of Structural and Functional Genomics, 2014Arabinose 5-phosphate (A5P) is the aldopentose version of the ketohexose fructose 6-phosphate (F6P), having identical stereochemistry but lacking atoms corresponding to the 1-carbon and 1-hydroxyl. Despite structural similarity and conservation of the reactive portion of F6P, F6P acts as a substrate whereas A5P is reported to be an inhibitor of ...
Samuel H, Light, Wayne F, Anderson
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L‐arabinose transport and the L‐arabinose binding protein of escherichia coli
Journal of Supramolecular Structure, 1977AbstractThe active accumulation of L‐arabinose by arabinose induced cultures of Escherichia coli is mediated by 2 independent transport mechanisms. One, specified by the gene locus araE, is membrane bound and possesses a relatively “low affinity.” The other, specified in part by the genetic locus araF, contains as a functional component the L‐arabinose
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1966
Publisher Summary This chapter discusses the determination of L-arabinose isomerase. L-arabinose isomerase activity is assayed spectrophotometrically at 30° using a standard spectrophotometer equipped with an absorbancy converter, automatic cuvette positioner, and recorder.
K. Yamanaka, W.A. Wood
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Publisher Summary This chapter discusses the determination of L-arabinose isomerase. L-arabinose isomerase activity is assayed spectrophotometrically at 30° using a standard spectrophotometer equipped with an absorbancy converter, automatic cuvette positioner, and recorder.
K. Yamanaka, W.A. Wood
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Biochemistry, 2012
AraC protein, which regulates expression of the l-arabinose operon in Escherichia coli, is a dimer whose DNA binding affinity for pairs of DNA half-sites is controlled by arabinose. Here we have addressed the question of whether the arabinose response of AraC requires the binding of one or two molecules of arabinose.
Michael E, Rodgers, Robert, Schleif
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AraC protein, which regulates expression of the l-arabinose operon in Escherichia coli, is a dimer whose DNA binding affinity for pairs of DNA half-sites is controlled by arabinose. Here we have addressed the question of whether the arabinose response of AraC requires the binding of one or two molecules of arabinose.
Michael E, Rodgers, Robert, Schleif
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