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Active transport of biotin in Escherichia coli K-12.
The transport of [(14)C]biotin into cells of a biotin prototroph, Escherichia coli K-12 strain Y10-1, was investigated. The vitamin taken up by the cells in this strain existed primarily in the freeExpand
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Biotinyl 5'-adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12.
A DNA filter-binding technique was used to study the interaction of the biotin repressor and operator site. From a biotin saturation curve, the concentration for half-maximal binding (K0.5) wasExpand
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The purification and properties of dethiobiotin synthetase.
Abstract The levels of dethiobiotin synthetase in Escherichia coli have been increased 6-fold over the wild type when prepared from a λ-lysogen carrying the bioD gene under phage control. TheExpand
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Purification and properties of 7, 8-diaminopelargonic acid aminotransferase.
The enzyme 7, 8-diaminopelargonic acid aminotransferase utilizes S-adenosyl-L-methionine to transaminate the biotin precurson 7-keto-8-aminopelargonic acid and form the next intermediate in theExpand
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Purification and properties of the biotin repressor. A bifunctional protein.
Definitive evidence is presented for the bifunctional nature of the biotin repressor protein which possesses both regulatory and enzymatic activities. The repressor protein can activate biotin in theExpand
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Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction.
The transamination of 7-keto-8-aminopelargonic acid by 7, 8-diaminopelargonic acid aminotransferase of Escherichia coli requires S-adenosyl-L-methionine as the amino donor. Initial velocity studiesExpand
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Dethiobiotin synthesis from 7,8-diaminolargonic acid in cell-free extracts of a biotin auxotroph of Escherichia coli K-12.
Abstract Dethiobiotin synthesis from 7,8-diaminopelargonic acid was demonstrated in cell-free extracts of Escherichia coli bioA mutants. The biosynthetically formed dethiobiotin was identified by itsExpand
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Mode of action of alpha-dehydrobiotin, a biotin analogue.
  • M. Eisenberg
  • Biology, Medicine
  • Journal of bacteriology
  • 1 July 1975
Alpha-Dehydrobiotin, like biotin, represses coordinately the 7,8-diaminopelargonic acid aminotransferase and the dethiobiotin synthetase enzymes that are encoded on the l and r strands, respectively,Expand
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Dethiobiotin synthetase.
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The kinetics of the amidase and esterase activities of trypsin.
In previous reports from this laboratory investigations of the specific esterase activity of trypsin (1) and of the detailed kinetics of the hydrolysis of specific substrates by chymotrypsin and byExpand
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