Biotin biosynthesis in higher plant cells

Baldet, Piérre; Gerbling, Heidrun; Axiotis, Stella; Douce, Roland

doi:10.1111/j.1432-1033.1993.tb18267.x

Cited by 86 publications

(60 citation statements)

References 32 publications

(17 reference statements)

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“…Similar results were obtained with B. sphaericus [24]. Further evidence supporting 9-mercaptodethiobiotin as an intermediate comes from experiments in which the label from [$%S]mercaptodethiobiotin was incorporated into biotin by a cell-free system from B. sphaericus [26], and the isolation of a reaction intermediate from plant cells that was proposed to be 9-mercaptodethiobiotin [27].…”

Section: Introductionsupporting

confidence: 67%

“…Many groups have tried to identify a reaction intermediate for biotin synthase, which would help to elucidate the reaction mechanism [24,25,27,35,36]. Our observation of an intermediate was made possible only by the use of the biotin synthase assay that we developed with ["%C]dethiobiotin as substrate.…”

Section: Implications and A Working Model For The Biotin Synthase Reamentioning

confidence: 99%

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Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use

Shaw

Birch

Tinschert

et al. 1998

Biochemical Journal

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A cell-free extract from Escherichia coli containing an E. coli biotin synthase that was expressed to approx. 1 % of soluble cell protein by cloning the E. coli bioB gene was used to investigate the biotin synthase reaction. The pH optimum was between 8 and 8n5, and the reaction velocity was dependent on the concentrations of dethiobiotin, cysteine, S-adenosylmethionine and asparagine. The catalytic-centre activity of the enzyme in itro was estimated to be 0n95 h −" , and each molecule of enzyme turned over less than one molecule of dethiobiotin, i.e. the enzyme was not acting catalytically. HPLC analysis of reaction mixtures revealed the presence of a compound with the characteristics of an intermediate : (1) it was labelled with "%C, and therefore derived from the ["%C]dethiobiotin substrate ; (2) it was present only in reaction mixtures containing biotin synthase ; (3) it was not derived from ["%C]biotin ; (4) $&S from [$&S]cystine was

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Section: Introductionsupporting

confidence: 67%

Section: Implications and A Working Model For The Biotin Synthase Reamentioning

confidence: 99%

Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use

Shaw

Birch

Tinschert

et al. 1998

Biochemical Journal

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“…Recently, Baldet et al reported that the conversion of dethiobiotin to biotin may proceed in two distinct steps involving 9-mercaptodethiobiotin as an intermediate in higher plant cells [30]. This intermediate may also be involved in biotin biosynthesis in bacteria including E. coli [31-331.…”

Section: Discussionmentioning

confidence: 99%

Flavodoxin is Required for Conversion of Dethiobiotin to Biotin in Escherichia coli

Ifuku

Koga

Haze

et al. 1994

European Journal of Biochemistry

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the enzymic conversion of dethiobiotin to biotin (catalyzed by the enzyme encoded by bioB) in cell-free extract of Escherichia coli which had been genetically engineered for high bioB expression. An unidentified protein(s) in addition to the bioB gene product is obligatory for this reaction. We have found that this protein was precipitated from the cell-free extract with poly(ethyleneimine), and we have purified it to homogeneity by a procedure which includes ammonium sulfate fractionation, DEAE-cellulose chromatography, gel filtration, and Mono Q chromatography. The apparent molecular mass of the purified protein was estimated to be about 21 kDa by SDSPAGE. The N-terminal amino acid sequence of the purified protein was identical with that of E. coli flavodoxin. We conclude that flavodoxin is required for conversion of dethiobiotin to biotin in E. coli. Studies with purified flavodoxin and the fraction containing the bioB gene product suggested that protein(s) in addition to the bioB gene product and flavodoxin is also obligatory for the reaction.

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“…5). The Bio2 enzyme is considered to be a rate-limiting enzyme in the biotin synthesis pathway (21). Because biotin-dependent carboxylases are involved in various processes such as energy metabolism, gluconeogenesis, and fatty acid synthesis in plants, it is believed that the need for biotin increases in light conditions rather than in dark conditions.…”

Section: Discussionmentioning

confidence: 99%

“…This step includes reactions that form a thiophene ring via the addition of a sulfur atom and is considered to be a rate-limiting step for biotin synthesis (21). In Arabidopsis, the expression of bio2 is reportedly regulated in response to development, light, the circadian period, and biotin starvation (16).…”

Section: Expression Of the Bio2 Gene In Pea Sprouts Is Suppressed Undmentioning

confidence: 99%

The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

Kamiyama

Ohnuki

Moriki

et al. 2016

J Nutr Sci Vitaminol

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Summary Biotin is an essential micronutrient, and is a cofactor for several carboxylases that are involved in the metabolism of glucose, fatty acids, and amino acids. Because plant cells can synthesize their own biotin, a wide variety of plant-based foods contains significant amounts of biotin; however, the influence of environmental conditions on the biotin content in plants remains largely unclear. In the present study, we investigated the effects of different cultivation conditions on the biotin content and biotin synthesis in pea sprouts (Pisum sativum Compared to the biotin content of pea sprouts under the control conditions, the biotin contents of pea sprouts under the low-light, dark, and cold conditions had significantly decreased. The dark group showed the lowest biotin content among the groups. Expression of the biotin synthase gene (bio2) was also significantly decreased under the dark and cold conditions compared to the control condition, in a manner similar to that observed for the biotin content. No significant differences in the adenosine triphosphate content were observed among the groups. These results indicate that environmental conditions such as light and temperature modulate the biotin content of pea plant tissues by regulating the expression of biotin synthase.

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Biotin biosynthesis in higher plant cells

Cited by 86 publications

References 32 publications

Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use

Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use

Flavodoxin is Required for Conversion of Dethiobiotin to Biotin in Escherichia coli

The Effects of Light and Temperature on Biotin Synthesis in Pea Sprouts

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