ライフサイエンスコーパス: adenosylcobalamin

1 ependent on the addition of the cofactor, 5'-adenosylcobalamin.

2 diol dehydratase as effectively as authentic adenosylcobalamin.

3 omponent in the absence or presence of bound adenosylcobalamin.

4 ivated cleavage of the cobalt-carbon bond of adenosylcobalamin.

5 sphorylate adenosylcobalamin-5'-phosphate to adenosylcobalamin.

6 presumed lower axial ligand to the cobalt of adenosylcobalamin.

7 ethylbenzimidazole nucleotide substituent of adenosylcobalamin.

8 glycine is predicted to block the binding of adenosylcobalamin.

9 ion of the unique organometalic Co-C bond of adenosylcobalamin.

10 on of vitamin B 12 into the active coenzyme, adenosylcobalamin.

11 the homolytic cleavage of the Co-C5' bond in adenosylcobalamin.

12 associated with the formation of 5'-dA from adenosylcobalamin.

13 abilization of the Co-C bond in enzyme-bound adenosylcobalamin.

14 earlier for the B(12) coenzymes, methyl- and adenosylcobalamin.

15 e to glutamate mutase initiates homolysis of adenosylcobalamin.

16 vely deuterated coenzyme, (5'R)-[5'-(2)H(1)] adenosylcobalamin (5'R/S = 3:1), was incubated with RTPR

17 ty of serovar Typhimurium to dephosphorylate adenosylcobalamin-5'-phosphate (AdoCbl-5'-P), the produc

18 alpha-ribazole, was shown to dephosphorylate adenosylcobalamin-5'-phosphate to adenosylcobalamin.

19 Adenosylcobalamin-5'-phosphate was also isolated from re

20 d CobT proteins resulted in the synthesis of adenosylcobalamin-5'-phosphate.

21 Adenosylcobalamin (Ado-B12) is both the cofactor and ind

22 des functions needed for the biosynthesis of adenosylcobalamin (Ado-B12).

23 n that this regulation occurs in response to adenosylcobalamin (Ado-Cbl) and operates primarily at th

24 cobalamin [CN-Cbl], aquocobalamin [H2O-Cbl], adenosylcobalamin [Ado-Cbl], and methylcobalamin [MeCbl]

25 ive hydrogels by covalently polymerizing the adenosylcobalamin (AdoB12)-dependent photoreceptor C-ter

26 diol by a pathway dependent on coenzyme B12 (adenosylcobalamin [AdoCb1]).

27 min and an escort that delivers the product, adenosylcobalamin (AdoCbl or coenzyme B(12)), to methylm

28 samples of diol dehydrase and the functional adenosylcobalamin (AdoCbl) analogue 5'-deoxy-3',4'-anhyd

29 Essential to biological activity of adenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl) i

30 uring the assembly of the nucleotide loop of adenosylcobalamin (AdoCbl) and other cobamides.

31 The coenzymes for 5,6-LAM are adenosylcobalamin (AdoCbl) and pyridoxal 5'-phosphate (P

32 ed"-state is required to bring the cofactors adenosylcobalamin (AdoCbl) and pyridoxal-5'-phosphate (P

33 h both the stoichiometry and apparent Kd for adenosylcobalamin (AdoCbl) are dependent upon the relati

34 RNR from Lactobacillus leichmannii utilizes adenosylcobalamin (AdoCbl) as a cofactor and, in additio

35 Breakdown of ethanolamine requires adenosylcobalamin (AdoCbl) as a cofactor, and, intriguin

36 bacillus leichmannii, a 76 kDa monomer using adenosylcobalamin (AdoCbl) as a cofactor, catalyzes the

37 leichmannii is a class II RNR that requires adenosylcobalamin (AdoCbl) as a cofactor.

38 olytic cleavage of the carbon-cobalt bond of adenosylcobalamin (AdoCbl) at a rate approximately 10(11

39 Characterization of the kinetics of adenosylcobalamin (AdoCbl) binding by stopped-flow fluor

40 In archaea and bacteria, the late steps in adenosylcobalamin (AdoCbl) biosynthesis are collectively

41 ylcobalamin (anAdoCbl) is an analogue of the adenosylcobalamin (AdoCbl) coenzyme.

42 mutase (MMCM) is an enzyme that utilizes the adenosylcobalamin (AdoCbl) cofactor to catalyze the rear

43 )] is an intermediate in the biosynthesis of adenosylcobalamin (AdoCbl) in many prokaryotes.

44 milar excited-state spectrum is observed for adenosylcobalamin (AdoCbl) in water and ethylene glycol.

45 same, except for the lower ligand, which in adenosylcobalamin (AdoCbl) is 5,6-dimethylbenzimidazole,

46 c acid by way of radical propagation from an adenosylcobalamin (AdoCbl) to a pyridoxal 5'-phosphate (

47 side 5'-triphosphates and uses coenzyme B12, adenosylcobalamin (AdoCbl), as a cofactor.

48 responsible for the de novo biosynthesis of adenosylcobalamin (AdoCbl), catalyzing the formation of

49 n mechanism of ornithine 4,5-aminomutase, an adenosylcobalamin (AdoCbl)- and pyridoxal L-phosphate (P

50 ylmalonyl-CoA mutase belongs to the class of adenosylcobalamin (AdoCbl)-dependent carbon skeleton iso

51 elated to those used for the reactivation of adenosylcobalamin (AdoCbl)-dependent diol dehydratase.

52 Methylmalonyl-CoA mutase is an adenosylcobalamin (AdoCbl)-dependent enzyme that catalyz

53 Methylmalonyl-CoA mutase is an 5'-adenosylcobalamin (AdoCbl)-dependent enzyme that catalyz

54 teady state of the reaction catalyzed by the adenosylcobalamin (AdoCbl)-dependent enzyme, methylmalon

55 e for (i) radical pair (RP) stabilization in adenosylcobalamin (AdoCbl)-dependent enzymes and (ii) th

56 is implicated in the catalytic cycles of all adenosylcobalamin (AdoCbl)-dependent enzymes, as in each

57 )alamin-5'-deoxyadenosyl radical pair in the adenosylcobalamin (AdoCbl)-dependent ethanolamine ammoni

58 the deamination of ethanolamine catalyzed by adenosylcobalamin (AdoCbl)-dependent ethanolamine ammoni

59 for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA m

60 PR) from Lactobacillus leichmannii catalyzes adenosylcobalamin (AdoCbl)-dependent nucleotide reductio

61 L-Methylmalonyl-CoA mutase (MUT) is an adenosylcobalamin (AdoCbl)-requiring mitochondrial matri

62 s (ACATs), implicated in the biosynthesis of adenosylcobalamin (AdoCbl).

63 Specifically, studied herein are the adenosylcobalamin (AdoCbl, also known as coenzyme B(12))

64 ) are enzymes that catalyze the formation of adenosylcobalamin (AdoCbl, coenzyme B(12)) from cobalami

65 r salvaging cobinamide (Cbi), a precursor of adenosylcobalamin (AdoCbl, coenzyme B(12)).

66 25 enzymes required for the biosynthesis of adenosylcobalamin (AdoCbl; coenzyme B(12) ).

67 )alamin formed by pulsed-laser photolysis of adenosylcobalamin (AdoCbl; coenzyme B(12)) in AdoCbl-dep

68 of how D-ornithine 4,5-aminomutase (OAM), an adenosylcobalamin (AdoCbl; coenzyme B(12))-dependent iso

69 ersion of vitamin B(12) into coenzyme B(12) (adenosylcobalamin, AdoCbl) is catalyzed by ATP:cob(I)ala

70 search, the mechanism by which coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent enzymes promote hom

71 1,2-propanediol (1,2-PD) in a coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent fashion.

72 the cofactor, substrate, and product in the adenosylcobalamin- (AdoCbl) dependent reaction of ethano

73 TPR) from Lactobacillus leichmannii utilizes adenosylcobalamin and catalyzes the conversion of nucleo

74 as formed by photolysis of the corresponding adenosylcobalamin and cryotrapped in glycerol-aqueous gl

75 Incubation of EAL with adenosylcobalamin and hydroxyethylhydrazine, an analogue

76 n glutamate mutase was reacted with [5'-(3)H]adenosylcobalamin and L-glutamate.

77 ne when the enzyme is reacted with [5'-(3)H]-adenosylcobalamin and L-glutamate.

78 The K(m) values for adenosylcobalamin and pyridoxal 5'-phosphate are 6.6 and

79 Lysine 5,6-aminomutase is an adenosylcobalamin and pyridoxal-5'-phosphate-dependent e

80 tric observations of both rapidly photolyzed adenosylcobalamin and the reaction of cob(III)alamin wit

81 he tritium exchange reaction between [5'-3H2]adenosylcobalamin and the solvent, confirming that the e

82 sylate de novo biosynthetic intermediates of adenosylcobalamin and to salvage incomplete and complete

83 tivation requires the presence of substrate, adenosylcobalamin, and PLP.

84 multaneously positioning the other cofactor, adenosylcobalamin, approximately 25 A from the active si

85 photoreceptors use a vitamin B12 derivative, adenosylcobalamin, as the light-sensing chromophore to m

86 cated on Cys 408 is generated by reaction of adenosylcobalamin at the active site and is proposed to

87 of cob(II)alamin and 5'-deoxyadenosine from adenosylcobalamin at the active site of dioldehydrase, a

88 (AdoB12)-dependent photoreceptor C-terminal adenosylcobalamin binding domain (CarHC) proteins using

89 vant cobinamide intermediates during de novo adenosylcobalamin biosynthesis are adenosylcobinamide-ph

90 cobY, however, failed to restore adenosylcobalamin biosynthesis in cobU mutants grown und

91 been proposed to catalyze the late steps in adenosylcobalamin biosynthesis, which define the nucleot

92 where growth of the cell depended on de novo adenosylcobalamin biosynthesis.

93 nosylcobinamide-GDP during the late steps of adenosylcobalamin biosynthesis.

94 hat this defect is not due to the absence of adenosylcobalamin but due to an inactive form of methylm

95 ly for cleavage of the cobalt-carbon bond of adenosylcobalamin by the enzyme, providing further suppo

96 the formation of the essential Co-C bond of adenosylcobalamin (coenzyme B 12) by transferring the ad

97 CobU is a bifunctional enzyme involved in adenosylcobalamin (coenzyme B(12)) biosynthesis in Salmo

98 The cleavage of adenosylcobalamin (coenzyme B(12)) to form cob(II)alamin

99 chemistry can be large and complex, such as adenosylcobalamin (coenzyme B(12)), simpler, such as S-a

100 g exogenous cobinamide (Cbi), a precursor of adenosylcobalamin (coenzyme B(12)).

101 The complex of dioldehydrase with adenosylcobalamin (coenzyme B12) and potassium ion react

102 novo corrin ring biosynthetic branch of the adenosylcobalamin (coenzyme B12) pathway of Salmonella e

103 The photolysis of adenosylcobalamin (coenzyme B12) results in homolytic cl

104 f isobutyryl-CoA mutase, in complex with the adenosylcobalamin cofactor and four different acyl-CoA s

105 ly labeled forms of the substrate and of the adenosylcobalamin cofactor.

106 The nrdJ gene encoding an O2-independent adenosylcobalamin-cofactored RNR was introduced into the

107 fted from its position in the substrate-free adenosylcobalamin complex.

108 periments with [(15)N-dimethylbenz-imidazole]adenosylcobalamin demonstrate base-off binding, consiste

109 pair catalytic intermediate in coenzyme B12 (adenosylcobalamin)-dependent ethanolamine ammonia-lyase

110 As a cofactor for adenosylcobalamin-dependent and methylcobalamin-dependen

111 arate is a substrate for the closely related adenosylcobalamin-dependent enzyme 2-methyleneglutarate

112 cam's Razor conclusion is that at least this adenosylcobalamin-dependent enzyme has not evolved to en

113 This adenosylcobalamin-dependent enzyme is postulated to gene

114 volutionary link between the radical SAM and adenosylcobalamin-dependent enzyme superfamilies.

115 Methylmalonyl-CoA mutase is an adenosylcobalamin-dependent enzyme that catalyzes the 1,

116 made of the mechanism of inactivation of the adenosylcobalamin-dependent enzyme, ethanolamine ammonia

117 Adenosylcobalamin-dependent enzymes accelerate the cleav

118 Adenosylcobalamin-dependent enzymes catalyze a variety o

119 A key step in the mechanism of all adenosylcobalamin-dependent enzymes is the abstraction o

120 Glutamate mutase is one of a group of adenosylcobalamin-dependent enzymes that catalyze a vari

121 Glutamate mutase is one of several adenosylcobalamin-dependent enzymes that catalyze unusua

122 Glutamate mutase is one of a group of adenosylcobalamin-dependent enzymes that catalyze unusua

123 Glutamate mutase is one of a group of adenosylcobalamin-dependent enzymes that catalyze unusua

124 the substrate, which is the next step in all adenosylcobalamin-dependent enzymes, the adenosyl radica

125 us isotope effect measurements made on other adenosylcobalamin-dependent enzymes.

126 coenzyme are key mechanistic features of all adenosylcobalamin-dependent enzymes.

127 Adenosylcobalamin-dependent glutamate mutase catalyzes a

128 action of adenosylcobalamin that occurs when adenosylcobalamin-dependent glutamate mutase is reacted

129 Adenosylcobalamin-dependent isomerases catalyze carbon s

130 iated with three subfamilies of enzymes: the adenosylcobalamin-dependent isomerases, the methylcobala

131 Adenosylcobalamin-dependent methylmalonyl-CoA mutase cat

132 Acyl-CoA mutases are a growing class of adenosylcobalamin-dependent radical enzymes that perform

133 affect coenzyme binding and catalysis in an adenosylcobalamin-dependent reaction.

134 of enzymatic mechanisms using free radicals, adenosylcobalamin-dependent reactions, the 5'-deoxyadeno

135 ydrogen transfer in a mechanism analogous to adenosylcobalamin-dependent reactions.

136 Methylmalonyl-CoA mutase catalyzes the adenosylcobalamin-dependent rearrangement of (2R)-methyl

137 The interaction of the adenosylcobalamin-dependent ribonucleoside diphosphate r

138 The adenosylcobalamin-dependent ribonucleoside triphosphate

139 A eutT+ gene provided in trans corrected the adenosylcobalamin-dependent transcription of a eut-lacZ

140 lytic intermediate state in coenzyme B(12)- (adenosylcobalamin-) dependent ethanolamine deaminase fro

141 Experiments with adenosylcobalamin enriched in (15)N in the dimethylbenzi

142 active form by addition of hydroxocobalamin/adenosylcobalamin, Fe(3+), and sulfide in the presence o

143 s dependent on the cofactor, coenzyme B12 or adenosylcobalamin, for activity.

144 to the remarkable functional repurposing of adenosylcobalamin from an enzyme cofactor to a light sen

145 in vitro assembly of the nucleotide loop of adenosylcobalamin from its precursors adenosylcobinamide

146 asurements of the dissociation constants for adenosylcobalamin from potassium-free (Kd = 16 +/- 2 mic

147 Adenosylcobalamin generated by this system supported the

148 y of the enzyme to catalyze the homolysis of adenosylcobalamin has been investigated using UV-visible

149 rt cobalamin to its biologically active form adenosylcobalamin has remained elusive.

150 This observation is consistent with adenosylcobalamin homolysis being slowed relative to hyd

151 ich allowed the pre-steady-state kinetics of adenosylcobalamin homolysis to be investigated by stoppe

152 Adenosylcobinamide was converted to adenosylcobalamin in reactions where all four enzymes we

153 the mechanism of the Co-C5' bond cleavage of adenosylcobalamin in the reaction of RTPR.

154 e synthesis of either R-methylmalonyl-CoA or adenosylcobalamin indicates that MeaB is necessary for p

155 , aqueous photoinduced homolytic cleavage of adenosylcobalamin, indicating that both reactions procee

156 -carbon bond in the biosynthetic pathway for adenosylcobalamin is catalyzed by the product of the cob

157 glutamate by 13-22-fold; K(m(apparent)) for adenosylcobalamin is little changed by these mutations.

158 The apparent Kd for adenosylcobalamin is raised by about 50-fold when His16

159 Tritiated adenosylcobalamin, labeled at the exchangeable position,

160 ese structures provide visualizations of how adenosylcobalamin mediates CarH tetramer formation in th

161 of the coenzyme, we examined the binding of adenosylcobalamin, methylcobalamin, and cob(II)alamin to

162 ure embodies a locking mechanism to keep the adenosylcobalamin out of the active site and prevent rad

163 the enzyme active site and with the product, adenosylcobalamin, partially occupied in the active site

164 vitamin B(12) through an oxygen-independent adenosylcobalamin pathway, which together with other key

165 ann domain would be free to rotate and bring adenosylcobalamin, pyridoxal-5'-phosphate, and substrate

166 y formed when aqueous, homolytically cleaved adenosylcobalamin reacts with molecular oxygen and provi

167 nthesis of the coenzyme form of vitamin B12, adenosylcobalamin, representing aerobic and anaerobic ro

168 proximities for cyclic-di-GMP, glycine, and adenosylcobalamin riboswitch aptamers without their liga

169 nylyltransferase activities (CobP in aerobic adenosylcobalamin synthesizers) to convert adenosylcobin

170 We describe a novel reaction of adenosylcobalamin that occurs when adenosylcobalamin-dep

171 tion state is essential for the synthesis of adenosylcobalamin, the coenzymic form of this cofactor.

172 s become significantly stiffer on going from adenosylcobalamin to 5'-deoxyadenosine, even though the

173 The cleavage of adenosylcobalamin to cob(III)alamin is accompanied by th

174 ope effects for the transfer of tritium from adenosylcobalamin to product in each direction.

175 e in the assembly of the nucleotide loop for adenosylcobalamin where it catalyzes both the phosphoryl