Bioconversion of Dethiobiotin into Biotin by Resting Cells and Protoplasts of<i>Bacillus sphaericus bioB</i>Transformant

Fujisawa, Ayumi; Abe, Takaharu; Ohsawa, I.; Shiozaki, Shozo; Kamogawa, K.; Izumi, Yoshikazu

doi:10.1271/bbb.57.740

Cited by 4 publications

(3 citation statements)

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“…20) In these strains, however, high expression of the biotin operon resulted in growth inhibition. Biotin overproduction has also been reported by other research groups in genetically engineered E. coli, 21,22) Bacillus sphaericus, 23,24) and Serratia marcescens, 25,26) and some of them have also observed growth inhibition 22 ,26) and plasmid instability23) due to overexpression of the biotin operon.…”

mentioning

confidence: 70%

Molecular Analysis of Growth Inhibition Caused by Overexpression of the Biotin Operon inEscherichia coli

Ifuku¹,

Koga²,

Haze³

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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mentioning

confidence: 70%

Molecular Analysis of Growth Inhibition Caused by Overexpression of the Biotin Operon inEscherichia coli

Ifuku¹,

Koga²,

Haze³

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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“…Two of the enzymes of the B. sphaericus pathway, pimeloyl coenzyme A (CoA) synthase and aminooxopelargonate synthase, have been expressed in E. coli and their characterization reported [12,13]. Cloning and overexpression of the bioB proteins of E. coli and B. sphaericus has also been achieved [14,15] and a recent report describes the purification and characterization of the E. coli enzyme [16].…”

Section: Introductionmentioning

confidence: 99%

Mechanistic implications and family relationships from the structure of dethiobiotin synthetase

1994

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This study establishes that the enzyme active site is situated at the dimer interface, with the substrate binding to one monomer and ATP to the other. The overall fold of DTBS closely resembles that of three other enzymes, adenylosuccinate synthetase (purA), Ha-ras-p21, and nitrogenase iron protein, that are unrelated by sequence or function, indicating that DTBS is a member of a diverse family of enzymes.

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“…Recombinant strains of E. coli (6,25), Bacillus sphaericus (11,19), and Serratia marcescens (26) that overproduce biotin were constructed previously by various groups interested in alternatives to the chemical synthesis of this vitamin. The R. meliloti strains constructed here represent the first attempt to use biotin synthesis genes to manipulate plant-microbe interactions.…”

Section: Discussionmentioning

confidence: 99%

Recombinant Rhizobium meliloti strains with extra biotin synthesis capability

Streit

Phillips

1996

Appl Environ Microbiol

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The growth of Rhizobium meliloti 1021 in an experimental alfalfa (Medicago sativa L.) rhizosphere was stimulated by adding nanomolar amounts of biotin. To overcome this biotin limitation, R. meliloti strains were constructed by conjugating the Escherichia coli biotin synthesis operon into biotin auxotroph R. meliloti 1021-B3. Transconjugant strains Rm1021-WS10 and Rm1021-WS11 grew faster in vitro and achieved a higher cell density than did R. meliloti 1021 and overproduced biotin on a defined medium. The increase in cell yield was associated with as much as a 99% loss in viability for Rm1021-WS11, but data suggested that a separate stabilizing factor in the E. coli DNA reduced cell death in Rm1021-WS10. In rhizosphere tests, the recombinant strains showed delayed growth and competed poorly against Rm1021.

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Bioconversion of Dethiobiotin into Biotin by Resting Cells and Protoplasts ofBacillus sphaericus bioBTransformant

Cited by 4 publications

References 0 publications

Molecular Analysis of Growth Inhibition Caused by Overexpression of the Biotin Operon inEscherichia coli

Molecular Analysis of Growth Inhibition Caused by Overexpression of the Biotin Operon inEscherichia coli

Mechanistic implications and family relationships from the structure of dethiobiotin synthetase

Recombinant Rhizobium meliloti strains with extra biotin synthesis capability

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