ライフサイエンスコーパス: biotin carboxylase

1 is communication between the two subunits of biotin carboxylase.

2 tuted with purified, recombinant Arabidopsis biotin carboxylase.

3 to several different reactions catalyzed by biotin carboxylase.

4 the substrate-induced synergism by biotin in biotin carboxylase.

5 c component are similar to those observed in biotin carboxylase.

6 etermined for D-alanine:D-alanine ligase and biotin carboxylase.

7 richia coli form of the enzyme consists of a biotin carboxylase activity, a biotin carboxyl carrier p

8 In comparison to wild-type biotin carboxylase, all four mutant enzymes gave very si

9 its: biotin carboxyl-carrier protein (BCCP), biotin carboxylase, alpha-carboxyltransferase, and beta-

10 the hypothesis that the two active sites of biotin carboxylase alternate their catalytic cycles.

11 ce identities (33-62%) to, respectively, the biotin carboxylase and biotin carboxyl carrier + carboxy

12 B- and C-domains, and in some cases, such as biotin carboxylase and carbamoyl phosphate synthetase, t

13 otein (holoBCCP87) to act as a substrate for biotin carboxylase and carboxyltransferase was assessed

14 acid synthesis and consists of two enzymes: biotin carboxylase and carboxyltransferase.

15 the X-ray crystal structure coordinates for biotin carboxylase and D-alanine:D-alanine ligase.

16 res of two mechanistically related proteins, biotin carboxylase and D-alanine:D-alanine ligase.

17 alpha-keto acid dehydrogenase E1 component, biotin carboxylase and superoxide dismutase were related

18 lear-coded subunits (biotin carboxy-carrier, biotin carboxylase, and alpha-carboxyltransferase).

19 yn is similar to D-alanine:D-alanine ligase, biotin carboxylase, and glutathione synthetase, despite

20 in vivo data indicate that both subunits of biotin carboxylase are required for activity and that th

21 r, structural data are available for E. coli biotin carboxylase as is a system for its overexpression

22 f the residues in the catalytic mechanism of biotin carboxylase as well as to establish a molecular b

23 The alpha-subunit contains the biotin carboxylase (BC) and biotin carboxyl carrier prot

24 Hints of a sub-complex between the biotin carboxylase (BC) and biotin carboxyl carrier prot

25 ylase (LmPC), a biotin-dependent enzyme with biotin carboxylase (BC) and carboxyltransferase (CT) act

26 ACC contains biotin carboxylase (BC) and carboxyltransferase (CT) act

27 ctions catalyzed by the holo-ACC components, biotin carboxylase (BC) and carboxyltransferase (CT), we

28 These enzymes share a conserved biotin carboxylase (BC) component, which catalyzes the A

29 roduct, is a nanomolar inhibitor against the biotin carboxylase (BC) domain of human, yeast, and othe

30 Biotin carboxylase (BC) is a conserved component among b

31 The biotin carboxylase (BC) subunit of Escherichia coli ACC

32 omponents that constitute plastid ACCase are biotin carboxylase (BC), biotin carboxyl carrier protein

33 The biotin carboxylase (BC), biotin carboxyl carrier protein

34 1.2) is a multisubunit complex consisting of biotin carboxylase (BC), biotin-carboxyl carrier protien

35 PC contains biotin carboxylase (BC), carboxyltransferase (CT) and bi

36 first enzymatic activity of the ACC complex, biotin carboxylase (BC), catalyzes the carboxylation of

37 t least four different protein subunits: the biotin carboxylase (BC), the biotin carboxyl carrier pro

38 dopyrimidines target the ATP-binding site of biotin carboxylase (BC), which catalyzes the first enzym

39 mposed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and

40 a coli acetyl-CoA carboxylase is composed of biotin carboxylase, carboxyltransferase and biotin carbo

41 nzyme consisting of three separate proteins: biotin carboxylase, carboxyltransferase, and the biotin

42 g of three distinct and separate components: biotin carboxylase, carboxyltransferase, and the biotin

43 id (pTrc.BCCP) encodes the C terminus of the biotin carboxylase carrier protein (BCCP) under the cont

44 in 1.3S contrasts with the findings for the biotin carboxylase carrier protein from E. coli acetyl-C

45 Biotin carboxylase catalyzes the ATP-dependent carboxyla

46 Biotin carboxylase catalyzes the ATP-dependent carboxyla

47 e three-dimensional structure of the E. coli biotin carboxylase complexed with ATP and determined to

48 The biotin carboxylase component catalyzes the ATP-dependent

49 The biotin carboxylase component catalyzes the ATP-dependent

50 The biotin carboxylase component has served for many years a

51 system for site-directed mutagenesis of the biotin carboxylase component is described.

52 The biotin carboxylase component, which catalyzes the ATP-de

53 Using the crystal structure of biotin carboxylase, cysteine 230 and lysine 238 were ide

54 The three-dimensional structure of biotin carboxylase, determined by x-ray crystallography,

55 In vitro kinetic studies of biotin carboxylase dimers in which both subunits were wi

56 osthetic group must first gain access to the biotin carboxylase domain and become carboxylated and th

57 mmetrical conformation in the absence of the biotin carboxylase domain and that the carboxyltransfera

58 The amino acid sequence of the biotin carboxylase domain encoded by Acc-1,1 and Acc-1,2

59 Fragments of genes encoding the biotin carboxylase domain of multidomain ACCs of T. gond

60 pyruvate and oxamate on the reactions of the biotin carboxylase domain.

61 In Escherichia coli, biotin carboxylase exists as a homodimer where each subu

62 Biotin carboxylase from Escherichia coli catalyzes the A

63 Expression of the mutant biotin carboxylase genes from an inducible arabinose pro

64 In the case of biotin carboxylase holoBCCP87 was an excellent substrate

65 The catalytic properties of the recombinant biotin carboxylase indicate that the activity of the het

66 The Escherichia coli biotin carboxylase is readily isolated from the other co

67 Numerical simulations of biotin carboxylase kinetics were the most similar to the

68 Four of these residues of biotin carboxylase, Lys-116, Lys-159, His-209, and Glu-2

69 However, kinetic assays of hybrid dimer biotin carboxylase molecules in which one subunit had an

70 whether novel ACCase inhibitors inhibit the biotin carboxylase or carboxyltransferase site of ACCase

71 richia coli form of the enzyme consists of a biotin carboxylase protein, a biotin carboxyl carrier pr

72 richia coli form of the enzyme consists of a biotin carboxylase protein, a biotin carboxyl carrier pr

73 The biotin carboxylase subunit of the heteromeric chloroplas

74 Holo-BCCP then interacts with the biotin carboxylase subunit, which leads to the addition

75 The M. tuberculosis genome contains three biotin carboxylase subunits (AccA1 to -3) and six carbox

76 tide probe representing conserved regions of biotin carboxylase subunits of acetyl coenzyme A (acetyl

77 d by the accA gene was strikingly similar to biotin carboxylase subunits of acetyl-CoA and propionyl-

78 se, which has an analogous mode of action to biotin carboxylase, suggests the catalytic base in this

79 e constructed three site-directed mutants of biotin carboxylase that are homologous to three missense

80 cherichia coli and the resulting recombinant biotin carboxylase was enzymatically active in carboxyla

81 y structure of an unliganded form of E. coli biotin carboxylase was originally solved in 1994 to 2.4-

82 bunit contributes to the overall function of biotin carboxylase, we made hybrid molecules in which on

83 ype, hybrid dimers, and mutant homodimers of biotin carboxylase were performed.

84 e mutants M169K, R338Q, and R338S of E. coli biotin carboxylase were selected for study to mimic the

85 y of the ATP synthesis reaction catalyzed by biotin carboxylase where carbamoyl phosphate reacts with

86 Stimulation of the ATP synthesis reaction of biotin carboxylase where carbamyl phosphate reacted with

87 A comparison of this closed form of biotin carboxylase with carbamoyl-phosphate synthetase i

88 The V/K or catalytic efficiency of biotin carboxylase with holoBCCP87 as substrate was 8000