Literature DB >> 7787312

Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli.

T Ohshiro1, M Yamamoto, B T Bui, D Florentin, A Marquet, Y Izumi.   

Abstract

The activity of biotin synthesis from dethiobiotin was found in cell-free extracts of an Escherichia coli bioB transformant. Among the sulfur compounds tested, only S-adenosyl-L-methionine (AdoMet) had a significant effect, while methionine and cysteine were inert. The activity was linearly stimulated by increasing protein concentration. When the dialyzed cell-free extracts were used for the reaction, NADP+, NADPH, and FAD among the well-known cofactors tested promoted the activity. Furthermore, in the presence of AdoMet, cysteine was apparently effective for biotin synthetic activity.

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Year:  1995        PMID： 7787312     DOI： 10.1271/bbb.59.943

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN： 0916-8451            Impact factor:   2.043


  3 in total

1.  Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions.

Authors:  N B Ugulava; B R Gibney; J T Jarrett
Journal:  Biochemistry       Date:  2001-07-27       Impact factor: 3.162

2.  Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters.

Authors:  N B Ugulava; B R Gibney; J T Jarrett
Journal:  Biochemistry       Date:  2000-05-02       Impact factor: 3.162

3.  Control of adenosylmethionine-dependent radical generation in biotin synthase: a kinetic and thermodynamic analysis of substrate binding to active and inactive forms of BioB.

Authors:  Natalia B Ugulava; Kendra K Frederick; Joseph T Jarrett
Journal:  Biochemistry       Date:  2003-03-11       Impact factor: 3.162
  3 in total

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