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

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

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

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

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

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

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

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

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

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

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

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

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

16 ect residues in the C-terminal region of the 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 enosylcobalamin (AdoCbl) to AdoCbl-dependent methylmalonyl-CoA mutase, an essential metabolic enzyme.

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

26 nt activity of propionyl-CoA carboxylase and methylmalonyl-CoA mutase and are life-threatening condit

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

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

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

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

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

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

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

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

35 impaired activity of the downstream enzymes, methylmalonyl-CoA mutase and methionine synthase.

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

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

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

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

40 Because methylmalonyl-CoA mutases are involved in the metabolism

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

42 Methylmalonyl-CoA mutase belongs to the class of adenosy

43 sential cofactor for methionine synthase and methylmalonyl-CoA mutase, but it must first undergo chem

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

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

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

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

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

49 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin

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

51 Methylmalonyl-CoA mutase catalyzes the isomerization of

52 Methylmalonyl-CoA mutase catalyzes the isomerization of

53 el with samples from various mouse models of methylmalonyl-CoA mutase deficiency.

54 ation of the enzymes methionine synthase and methylmalonyl-CoA mutase, disrupting gene expression and

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

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

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

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

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

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

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

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

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

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

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

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

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

68 Methylmalonyl-CoA mutase is a key enzyme in intermediary

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

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

71 Methylmalonyl-CoA mutase is an adenosylcobalamin (AdoCbl

72 Methylmalonyl-CoA mutase is an adenosylcobalamin-depende

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

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

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

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

77 tive, itaconyl-CoA, inhibits B(12)-dependent methylmalonyl-CoA mutase (MCM) by an unknown mechanism.

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

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

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

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

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

83 he delivery of adenosylcobalamin (AdoCbl) to methylmalonyl-CoA mutase (MCM), the only AdoCbl-dependen

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

85 so serves as an escort, delivering AdoCbl to methylmalonyl-CoA mutase (MCM).

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

87 Our AAV vector was designed to insert a methylmalonyl-CoA mutase (MMUT) transgene into the 3' en

88 In these cells, the B(12)-dependent enzyme, methylmalonyl-CoA mutase (MMUT), plays a central role in

89 delivery and repair of B(12)-dependent human methylmalonyl-CoA mutase (MMUT).

90 oxidation-like pathways as well as inhibited methylmalonyl-CoA mutase (MUT) at lower doses.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

106 sets showed cystathionine beta synthase and methylmalonyl-CoA-mutase to be common to 3 out of 4 data

107 rone that escorts AdoCbl, transferring it to methylmalonyl-CoA mutase, which is important in propiona