ライフサイエンスコーパス: biotin synthase

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 MybB thus represents a generalization of biotin synthase activity that contributes to the maturat

5 g or for PLP-induced cysteine desulfurase or biotin synthase activity was observed with any of the fo

6 omolytic cleavage of C-H or C-C bonds, i.e., biotin synthase, anaerobic ribonucleotide reductase, pyr

7 Two enzymes active in these pathways, biotin synthase and glutamate synthase, require an iron-

8 Biotin synthase and lipoate synthase are SAM-dependent [

9 es involved in thiolation reactions, such as biotin synthase and lipoate synthase, is discussed as we

10 MybB is a homologue of biotin synthase, and in both biosynthetic pathways, the

11 onic strength: in the positive ion spectrum, biotin synthase at low ionic strength (pH 7.0-8.5) yield

12 uberculosis requires Rv1590 (which we named "biotin synthase auxiliary protein" or BsaP), for activit

13 and recent experimental results suggest that biotin synthase belongs to a family of enzymes that cont

14 The single Arabidopsis gene coding for biotin synthase, BIO2, was isolated and sequenced.

15 Biotin synthase (BioB) converts dethiobiotin into biotin

16 ituted forms of recombinant Escherichia coli biotin synthase (BioB) has been investigated using the c

17 Biotin synthase (BioB) is a member of the Radical SAM su

18 Biotin synthase (BioB) is aerobically purified as a dime

19 Biotin synthase (BioB) is aerobically purified as a dime

20 Biotin synthase (BioB) is aerobically purified as a dime

21 Biotin synthase (BioB) is an iron-sulfur enzyme that cat

22 The recently resolved X-ray structure of biotin synthase (BioB) was used to guide the multiple se

23 ethiobiotin to biotin, which is catalyzed by biotin synthases (BioB).

24 Biotin synthase (BS) catalyzes the oxidative addition of

25 Biotin synthase (BS) is an AdoMet-dependent radical enzy

26 Biotin synthase (BS) is an S-adenosylmethionine (AdoMet)

27 s cDNA was shown to code for the Arabidopsis biotin synthase by its ability to complement a bioB muta

28 Biotin synthase catalyzes formation of the thiophane rin

29 Biotin synthase catalyzes the conversion of dethiobiotin

30 Biotin synthase catalyzes the insertion of a sulfur atom

31 Biotin synthase catalyzes the insertion of a sulfur atom

32 Biotin synthase catalyzes the oxidative addition of a su

33 Biotin synthase catalyzes the radical-mediated insertion

34 The biotin synthase coding sequence is interrupted by five i

35 Biotin synthase contains a highly conserved sequence mot

36 and to better understand the manner in which biotin synthase controls radical generation and reactivi

37 The crystal structure of biotin synthase from Escherichia coli in complex with S-

38 Biotin synthase from Escherichia coli was analyzed by na

39 s sequence similarity to the carboxyl end of biotin synthase from Escherichia coli was used to isolat

40 abidopsis biotin synthase is most similar to biotin synthases from E. coli, Serratia marcescens, and

41 that was homologous to the Escherichia coli biotin synthase gene (BioB).

42 . 2:1:1 AdoMet:DTB:BS dimer, suggesting that biotin synthase has a single functional active site per

43 Fe-S cluster in recombinant Escherichia coli biotin synthase have been investigated in as-prepared an

44 sequence from BIO2 with bacterial and yeast biotin synthase homologs revealed a high degree of seque

45 ish the predominant cluster forms present in biotin synthase in anaerobic assays, and by inference in

46 e that the dominant stable cluster state for biotin synthase is a dimer containing two [2Fe-2S](2+) a

47 Biotin synthase is a member of the radical SAM superfami

48 Biotin synthase is a radical S-adenosylmethionine (SAM)

49 oxyadenosine and methionine, suggesting that biotin synthase is an AdoMet-dependent radical enzyme.

50 Biotin synthase is an iron-sulfur protein that utilizes

51 This kinetic analysis suggests that biotin synthase is evolved to bind AdoMet both weakly an

52 The primary sequence of the Arabidopsis biotin synthase is most similar to biotin synthases from

53 threonine-173, which is highly conserved in biotin synthases, is important for catalytic competence

54 ized as homologs are lysine 2,3-aminomutase, biotin synthase, lipoic acid synthase and the activating

55 ymes that catalyze sulfur insertion, such as biotin synthase, lipoyl synthase, and MiaB.

56 nce of the amino terminus of the Arabidopsis biotin synthase may represent an organelle-targeting tra

57 o the appropriate target apoproteins such as biotin synthase, perhaps by enhancing or prolonging the

58 ation of anaerobic ribonucleotide reductase, biotin synthase, pyruvate formate lyase, and cobalamin-d

59 iated biotin synthases with BsaP-independent biotin synthases suggest that the need for BsaP is deter

60 Binding of Cu2+ to biotin synthase was also observed; in the presence of ex

61 e coordination of the iron-sulfur cluster in biotin synthase was obtained in a tandem mass spectromet

62 h this dual role for iron-sulfur clusters in biotin synthase, we have found that the protein is stabl

63 Structural comparisons of BsaP-associated biotin synthases with BsaP-independent biotin synthases