ライフサイエンスコーパス: carboxyltransferase

1 rboxy-carrier, biotin carboxylase, and alpha-carboxyltransferase).

2 oxylase, alpha-carboxyltransferase, and beta-carboxyltransferase.

3 t in an operon, yet yield an alpha(2)beta(2) carboxyltransferase.

4 sists of two enzymes: biotin carboxylase and carboxyltransferase.

5 sing a known bisubstrate analog inhibitor of carboxyltransferase.

6 xylase, biotin carboxyl carrier protein, and carboxyltransferase.

7 desthiobiotin and 2-imidazolidone, inhibited carboxyltransferase.

8 tein, and the alpha and beta subunits of the carboxyltransferase.

9 oduced in 5S result in a similar decrease in carboxyltransferase activity and crystal structures with

10 In this case, inhibition of the carboxyltransferase activity of ACCase (second half-reac

11 yltransferase domain, and therefore that the carboxyltransferase activity of ACCase (second half-reac

12 ty, a biotin carboxyl carrier protein, and a carboxyltransferase activity.

13 ose an unusual regulatory mechanism by which carboxyltransferase acts as a 'dimmer switch' to regulat

14 (BCCP), and the alpha- and beta-subunits of carboxyltransferase (alpha- and beta-CT).

15 To further characterize the carboxyltransferase, an improved assay for CT was develo

16 e primary structure of the Arabidopsis alpha-carboxyltransferase and beta-carboxyltransferase subunit

17 ipitation experiments confirm that the alpha-carboxyltransferase and beta-carboxyltransferase subunit

18 rboxylase is composed of biotin carboxylase, carboxyltransferase and biotin carboxyl carrier protein

19 composed of one plastid-coded subunit (beta-carboxyltransferase) and three nuclear-coded subunits (b

20 er protein (BCCP), biotin carboxylase, alpha-carboxyltransferase, and beta-carboxyltransferase.

21 three separate proteins: biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier pro

22 and separate components: biotin carboxylase, carboxyltransferase, and the biotin carboxyl carrier pro

23 The steady-state kinetics of the recombinant carboxyltransferase are characterized in the reverse dir

24 e biocytin and the binding of malonyl-CoA to carboxyltransferase at equilibrium.

25 Carboxyltransferase binds the coding regions of both sub

26 The rate of inactivation of carboxyltransferase by N-ethylmaleimide decreased with d

27 port the overexpression of the genes for the carboxyltransferase component is described.

28 ACC contains biotin carboxylase (BC) and carboxyltransferase (CT) activities, and its biotin is l

29 dent enzyme with biotin carboxylase (BC) and carboxyltransferase (CT) activities.

30 and kill sensitive plants by inhibiting the carboxyltransferase (CT) activity of ACC.

31 mains, whereas the beta-subunit supplies the carboxyltransferase (CT) activity.

32 PC contains biotin carboxylase (BC), carboxyltransferase (CT) and biotin carboxyl carrier pro

33 an admT gene with homology to the acetyl-CoA carboxyltransferase (CT) beta-subunit gene accD.

34 The carboxyltransferase (CT) domain of ACC is the site of ac

35 The carboxyltransferase (CT) domain of this enzyme is the si

36 ure-based inhibitor design, particularly the carboxyltransferase (CT) domain, which is the primary si

37 eral herbicides function by inhibiting their carboxyltransferase (CT) domain.

38 The AccA and AccD subunits form the carboxyltransferase (CT) heterotetramer that catalyzes t

39 The bacterial carboxyltransferase (CT) subunit of ACC is a target for

40 in carboxyl carrier protein (BCCP), and beta-carboxyltransferase (CT) subunits of the plastidial-ACCa

41 -ACC components, biotin carboxylase (BC) and carboxyltransferase (CT), were simultaneously monitored

42 f the biotin carboxylase domain and that the carboxyltransferase domain active site is conformational

43 A 5S-based homology model of the PC carboxyltransferase domain indicates a conserved mechani

44 bstrate-induced biotin binding pocket in the carboxyltransferase domain of PC from Rhizobium etli.

45 th aryloxyphenoxypropionates showed that the carboxyltransferase domain of the apicoplast T. gondii A

46 cDNA fragments encoding the carboxyltransferase domain of the multidomain plastid ac

47 ite are highly conserved with respect to the carboxyltransferase domain of the Streptomyces coelicolo

48 Structures of the carboxyltransferase domain reveal that R. etli PC occupi

49 uggest that this region includes part of the carboxyltransferase domain, and therefore that the carbo

50 ome carboxylated and then translocate to the carboxyltransferase domain, where the carboxyl group is

51 ted close to a highly conserved motif of the carboxyltransferase domain, which is probably a part of

52 Given the conservation with carboxyltransferase domains in oxaloacetate decarboxylas

53 CC-B subunit shows the highest similarity to carboxyltransferase domains of biotin enzymes that use m

54 in carboxylase and biotin carboxyl carrier + carboxyltransferase domains or subunits of known biotin-

55 ACCases, M. tuberculosis contains six ACCase carboxyltransferase domains, AccD1-6, whose specific rol

56 The plant alpha-carboxyltransferases have gained a C-terminal domain rel

57 o-N,N-dibenzyloxazole-5-carboxamide, and the carboxyltransferase inhibitor, andrimid, was confirmed u

58 in, a biotin carboxyl carrier protein, and a carboxyltransferase protein.

59 in, a biotin carboxyl carrier protein, and a carboxyltransferase protein.

60 The carboxyltransferase reaction was assayed in the reverse

61 Here, we report that carboxyltransferase regulates its own translation by bin

62 inhibitors inhibit the biotin carboxylase or carboxyltransferase site of ACCase.

63 The carboxyltransferase subunit catalyzes the transfer of a

64 h-throughput screening for inhibitors of the carboxyltransferase subunit.

65 nzyme activity assay for the isolated AccAD (carboxyltransferase) subunit, which is useful for determ

66 n carboxylase subunits (AccA1 to -3) and six carboxyltransferase subunits (AccD1 to -6), with accD6 l

67 that the alpha-carboxyltransferase and beta-carboxyltransferase subunits are physically associated.

68 abidopsis alpha-carboxyltransferase and beta-carboxyltransferase subunits deduced from nucleotide seq

69 wed high degrees of sequence similarity with carboxyltransferase subunits of acetyl-CoA and propionyl

70 ding domains, which are conserved in several carboxyltransferase subunits of acyl-CoA carboxylases, w

71 Preferential binding of carboxyltransferase to RNA in situ was shown using fluor

72 ct as a substrate for biotin carboxylase and carboxyltransferase was assessed and compared with the r

73 The interaction of holoBCCP87 with carboxyltransferase was characterized in the reverse dir

74 Carboxyltransferase was inactivated by N-ethylmaleimide,

75 The V/K or catalytic efficiency of carboxyltransferase with holoBCCP87 as substrate is 2000