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1 e binding of AdoMet and DTB to reconstituted biotin synthase.
2 iron-sulfur clusters may play a dual role in biotin synthase: a reduced iron-sulfur cluster is probab
3                                           In biotin synthase, abstraction of a hydrogen atom from the
4 g or for PLP-induced cysteine desulfurase or biotin synthase activity was observed with any of the fo
5 omolytic cleavage of C-H or C-C bonds, i.e., biotin synthase, anaerobic ribonucleotide reductase, pyr
6        Two enzymes active in these pathways, biotin synthase and glutamate synthase, require an iron-
7                                              Biotin synthase and lipoate synthase are SAM-dependent [
8 es involved in thiolation reactions, such as biotin synthase and lipoate synthase, is discussed as we
9 onic strength: in the positive ion spectrum, biotin synthase at low ionic strength (pH 7.0-8.5) yield
10 and recent experimental results suggest that biotin synthase belongs to a family of enzymes that cont
11       The single Arabidopsis gene coding for biotin synthase, BIO2, was isolated and sequenced.
12                                              Biotin synthase (BioB) converts dethiobiotin into biotin
13 ituted forms of recombinant Escherichia coli biotin synthase (BioB) has been investigated using the c
14                                              Biotin synthase (BioB) is aerobically purified as a dime
15                                              Biotin synthase (BioB) is aerobically purified as a dime
16                                              Biotin synthase (BioB) is aerobically purified as a dime
17                                              Biotin synthase (BioB) is an iron-sulfur enzyme that cat
18     The recently resolved X-ray structure of biotin synthase (BioB) was used to guide the multiple se
19                                              Biotin synthase (BS) catalyzes the oxidative addition of
20                                              Biotin synthase (BS) is an AdoMet-dependent radical enzy
21                                              Biotin synthase (BS) is an S-adenosylmethionine (AdoMet)
22 s cDNA was shown to code for the Arabidopsis biotin synthase by its ability to complement a bioB muta
23                                              Biotin synthase catalyzes formation of the thiophane rin
24                                              Biotin synthase catalyzes the conversion of dethiobiotin
25                                              Biotin synthase catalyzes the insertion of a sulfur atom
26                                              Biotin synthase catalyzes the insertion of a sulfur atom
27                                              Biotin synthase catalyzes the oxidative addition of a su
28                                              Biotin synthase catalyzes the radical-mediated insertion
29                                          The biotin synthase coding sequence is interrupted by five i
30                                              Biotin synthase contains a highly conserved sequence mot
31 and to better understand the manner in which biotin synthase controls radical generation and reactivi
32                     The crystal structure of biotin synthase from Escherichia coli in complex with S-
33                                              Biotin synthase from Escherichia coli was analyzed by na
34 s sequence similarity to the carboxyl end of biotin synthase from Escherichia coli was used to isolat
35 abidopsis biotin synthase is most similar to biotin synthases from E. coli, Serratia marcescens, and
36  that was homologous to the Escherichia coli biotin synthase gene (BioB).
37 . 2:1:1 AdoMet:DTB:BS dimer, suggesting that biotin synthase has a single functional active site per
38 Fe-S cluster in recombinant Escherichia coli biotin synthase have been investigated in as-prepared an
39  sequence from BIO2 with bacterial and yeast biotin synthase homologs revealed a high degree of seque
40 ish the predominant cluster forms present in biotin synthase in anaerobic assays, and by inference in
41 e that the dominant stable cluster state for biotin synthase is a dimer containing two [2Fe-2S](2+) a
42                                              Biotin synthase is a member of the radical SAM superfami
43                                              Biotin synthase is a radical S-adenosylmethionine (SAM)
44 oxyadenosine and methionine, suggesting that biotin synthase is an AdoMet-dependent radical enzyme.
45                                              Biotin synthase is an iron-sulfur protein that utilizes
46          This kinetic analysis suggests that biotin synthase is evolved to bind AdoMet both weakly an
47      The primary sequence of the Arabidopsis biotin synthase is most similar to biotin synthases from
48  threonine-173, which is highly conserved in biotin synthases, is important for catalytic competence
49 ized as homologs are lysine 2,3-aminomutase, biotin synthase, lipoic acid synthase and the activating
50 ymes that catalyze sulfur insertion, such as biotin synthase, lipoyl synthase, and MiaB.
51 nce of the amino terminus of the Arabidopsis biotin synthase may represent an organelle-targeting tra
52 o the appropriate target apoproteins such as biotin synthase, perhaps by enhancing or prolonging the
53 ation of anaerobic ribonucleotide reductase, biotin synthase, pyruvate formate lyase, and cobalamin-d
54                           Binding of Cu2+ to biotin synthase was also observed; in the presence of ex
55 e coordination of the iron-sulfur cluster in biotin synthase was obtained in a tandem mass spectromet
56 h this dual role for iron-sulfur clusters in biotin synthase, we have found that the protein is stabl

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