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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
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
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
13 ituted forms of recombinant Escherichia coli biotin synthase (BioB) has been investigated using the c
18 The recently resolved X-ray structure of biotin synthase (BioB) was used to guide the multiple se
22 s cDNA was shown to code for the Arabidopsis biotin synthase by its ability to complement a bioB muta
31 and to better understand the manner in which biotin synthase controls radical generation and reactivi
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
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
44 oxyadenosine and methionine, suggesting that biotin synthase is an AdoMet-dependent radical enzyme.
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
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
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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