ライフサイエンスコーパス: methylmalonyl-CoA mutase

1 the vitamin B12 (cobalamin)-dependent enzyme methylmalonyl CoA mutase.

2 yl CoA:succinate CoA transferase, and Sbm is methylmalonyl CoA mutase.

3 cofactor required by methionine synthase and methylmalonyl-CoA mutase.

4 um extorquens MeaB, which is a chaperone for methylmalonyl-CoA mutase.

5 dent target enzymes, methionine synthase and methylmalonyl-CoA mutase.

6 rotein interaction with its partner protein, methylmalonyl-CoA mutase.

7 n and assembly of the B(12)-dependent enzyme methylmalonyl-CoA mutase.

8 eaction catalyzed by the radical B12 enzyme, methylmalonyl-CoA mutase.

9 hich is stimulated approximately 100-fold by methylmalonyl-CoA mutase.

10 product Co2+ Cbl) is modulated by the enzyme methylmalonyl-CoA mutase.

11 osylcobalamin but due to an inactive form of methylmalonyl-CoA mutase.

12 M3 and M2 labeled, reflecting reversal of S-methylmalonyl-CoA mutase.

13 ted with the homolysis reaction catalyzed by methylmalonyl-CoA mutase.

14 be a significant contributor to catalysis by methylmalonyl-CoA mutase.

15 ect residues in the C-terminal region of the methylmalonyl-CoA mutase.

16 2-dependent enzymes, methionine synthase and methylmalonyl-CoA mutase.

17 oop GTPase and are currently misannotated as methylmalonyl-CoA mutases.

18 Methylmalonyl-CoA mutase accelerates the rate of Co-C bo

19 We found that nitric oxide (NO) inhibits methylmalonyl-CoA mutase activity in rodent cell extract

20 r inhibiting cellular NO synthesis increased methylmalonyl-CoA mutase activity when measured subseque

21 Methylobacterium extorquens, which supports methylmalonyl-CoA mutase activity, serves dual functions

22 mutase and a recently characterized archaeal methylmalonyl-CoA mutase, allowed demonstration of its r

23 ction of the radical B(12)-dependent enzyme, methylmalonyl-CoA mutase, although its precise role is n

24 We show that methylmalonyl-CoA mutase, an R-specific crotonase, isobu

25 In the presence of methylmalonyl-CoA mutase and ATP, AdoCbl is transferred

26 nction of two crucial enzymes, mitochondrial methylmalonyl-CoA mutase and cytosolic methionine syntha

27 cluding adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have

28 In contrast, trans ligand effects in methylmalonyl-CoA mutase and indeed the significance of

29 ich catalyze carbon skeleton rearrangements, methylmalonyl-CoA mutase and isobutyryl-CoA mutase (ICM)

30 However, both methylmalonyl-CoA mutase and isobutyryl-CoA mutase, whic

31 The dissociation constant for binding of methylmalonyl-CoA mutase and MeaB ranges from 34 +/- 4 t

32 cs of interaction between the radical enzyme methylmalonyl-CoA mutase and MeaB, which are discussed.

33 on the kinetics of the reaction catalyzed by methylmalonyl-CoA mutase and on the thermodynamics of co

34 is to create the H610A and H610N variants of methylmalonyl-CoA mutase and report that both mutations

35 demonstrated that MeaB forms a complex with methylmalonyl-CoA mutase and stimulates in vitro mutase

36 Thus, NO inhibition of methylmalonyl-CoA mutase appeared to be from the reactio

37 Because methylmalonyl-CoA mutases are involved in the metabolism

38 ability of the double mutant (Y89F/R207Q) of methylmalonyl-CoA mutase as well as of the single mutant

39 Methylmalonyl-CoA mutase belongs to the class of adenosy

40 The inhibition of methylmalonyl-CoA mutase by NO was likely of physiologic

41 tion of Co-carbon bond homolysis rate in the methylmalonyl-CoA mutase-catalyzed reaction has been eva

42 ion of the active site residue, R207, in the methylmalonyl-CoA mutase-catalyzed reaction.

43 ct a qualitative free energy profile for the methylmalonyl-CoA mutase-catalyzed reaction.

44 rk, to investigate the initial stages of the methylmalonyl-CoA-mutase-catalyzed reaction.

45 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin

46 Adenosylcobalamin-dependent methylmalonyl-CoA mutase catalyzes the interconversion o

47 Methylmalonyl-CoA mutase catalyzes the isomerization of

48 Methylmalonyl-CoA mutase catalyzes the isomerization of

49 Inherited defects in the gene for methylmalonyl-CoA mutase (EC 5.4.99.2) result in the mut

50 he hypothesis that MeaB functions to protect methylmalonyl-CoA mutase from irreversible inactivation.

51 MeaB and methylmalonyl-CoA mutase from M. extorquens were cloned

52 dicted gene product showed 35% identity with methylmalonyl-CoA mutases from various sources.

53 e of the better characterized and homologous methylmalonyl-CoA mutase/G-protein chaperone system.

54 CoA, we inferred that conserved neighbors of methylmalonyl-CoA mutase genes and their human homologue

55 at were frequently arranged with prokaryotic methylmalonyl-CoA mutase genes, and that were of unknown

56 adenosylcobalamin (AdoCbl)-dependent enzyme, methylmalonyl-CoA mutase, has been studied.

57 cobalamin-dependent methionine synthase and methylmalonyl-CoA mutase have revealed a striking confor

58 rward direction by reducing the ratio of apo-methylmalonyl-CoA mutase/holo-ATR required for delivery

59 X-ray crystal structures of methylmalonyl-CoA mutase in complexes with substrate met

60 he presence and absence of nucleotides) with methylmalonyl-CoA mutase (in the presence and absence of

61 usly for the related Cbl-dependent isomerase methylmalonyl-CoA mutase indicate that a common mechanis

62 Methylmalonyl-CoA mutase is a key enzyme in intermediary

63 Methylmalonyl-CoA mutase is a member of the family of co

64 Methylmalonyl-CoA mutase is an 5'-adenosylcobalamin (Ado

65 Methylmalonyl-CoA mutase is an adenosylcobalamin (AdoCbl

66 Methylmalonyl-CoA mutase is an adenosylcobalamin-depende

67 yadenosylcobalamin by adenosyltransferase to methylmalonyl-CoA mutase is gated by a small G protein,

68 This study shows that methylmalonyl-CoA mutase is induced by several stresses,

69 significant amino acid sequence identity to methylmalonyl-CoA mutase (MCM) (40%) and isobutyryl-CoA

70 tive 5'-deoxyadenosylcobalamin cofactor onto methylmalonyl-CoA mutase (MCM) and precludes loading of

71 The methylmalonyl-CoA mutase (MCM) cDNA was highly expressed

72 Within this family, methylmalonyl-CoA mutase (MCM) is the best studied and i

73 mans, deficiencies in coenzyme B12-dependent methylmalonyl-CoA mutase (MCM) lead to methylmalonyl aci

74 of bacterial and mitochondrial B12-dependent methylmalonyl-CoA mutase (MCM), HCM has a highly conserv

75 osylcobalamin (AdoCbl or coenzyme B(12)), to methylmalonyl-CoA mutase (MCM), resulting in holoenzyme

76 tion of 5'-deoxyadenosyl cobalamin-dependent methylmalonyl-CoA mutase (MCM).

77 Methylmalonyl-CoA mutase (MMCM) is an enzyme that utiliz

78 L-Methylmalonyl-CoA mutase (MUT) is an adenosylcobalamin (

79 f metabolism caused by defective activity of methylmalonyl-CoA mutase (MUT) that exhibits multiorgan

80 ed by deficiency of the mitochondrial enzyme methylmalonyl-CoA mutase (MUT), is often complicated by

81 aciduria (MMAuria), caused by deficiency of methylmalonyl-CoA mutase (MUT), usually presents in the

82 inhibitor of the mitochondrial B12-dependent methylmalonyl-CoA mutase (MUT).

83 thesis pathway and the vitamin B12-dependent methylmalonyl-CoA-mutase MutAB.

84 alonyl-CoA supplied in vivo by the AtoAD and methylmalonyl-CoA mutase pathways, respectively, to prod

85 m under all conditions tested, and (iii) the methylmalonyl-CoA mutase reaction is reversible, but its

86 he essential enzymes methionine synthase and methylmalonyl-CoA mutase, respectively.

87 four-gene operon that encodes homologues of methylmalonyl CoA mutases (Sbm) and acyl CoA transferase

88 This portion of the methylmalonyl-CoA mutase sequence can be aligned with re

89 ace of the protein where its partner protein methylmalonyl-CoA mutase should bind.

90 m a primary CH(3)- group in AdoCbl-dependent methylmalonyl-CoA mutase shows the enzymic and enzyme-fr

91 ism is demonstrated by a patient mutation in methylmalonyl-CoA mutase that does not impair the activi

92 The alignments allow the mutations of human methylmalonyl-CoA mutase to be mapped onto the structure