ライフサイエンスコーパス: adenosylcobalamin

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

2 e to glutamate mutase initiates homolysis of adenosylcobalamin.

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

4 diol dehydratase as effectively as authentic adenosylcobalamin.

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

6 sphorylate adenosylcobalamin-5'-phosphate to adenosylcobalamin.

7 omponent in the absence or presence of bound adenosylcobalamin.

8 presumed lower axial ligand to the cobalt of adenosylcobalamin.

9 ethylbenzimidazole nucleotide substituent of adenosylcobalamin.

10 glycine is predicted to block the binding of adenosylcobalamin.

11 uicide inactivator that forms an adduct with adenosylcobalamin.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

48 GTP hydrolysis to facilitate the delivery of adenosylcobalamin (AdoCbl) to AdoCbl-dependent methylmal

49 responsible for facilitating the delivery of adenosylcobalamin (AdoCbl) to methylmalonyl-CoA mutase (

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

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

52 , trafficking, or derivatization to 5'-deoxy-adenosylcobalamin (AdoCbl), the required MUT cofactor.

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

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

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

56 The adenosylcobalamin (AdoCbl)-dependent enzyme ethanolamine

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

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

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

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

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

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

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

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

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

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

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

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

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

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

71 25 enzymes required for the biosynthesis of adenosylcobalamin (AdoCbl; coenzyme B(12) ).

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

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

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

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

76 1,2-propanediol (1,2-PD) in a coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent fashion.

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

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

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

80 Incubation of EAL with adenosylcobalamin and hydroxyethylhydrazine, an analogue

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

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

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

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

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

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

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

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

89 catalyzes the conversion of vitamin B(12) to adenosylcobalamin, and whose expression has previously b

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

114 tion of four bioactive forms of vitamin B12 (adenosylcobalamin, cyanocobalamin, hydroxocobalamin, met

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

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

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

118 n radical-based transformations catalyzed by adenosylcobalamin-dependent and radical S-adenosyl-l-met

119 ucleoside triphosphate reducers, whereas the adenosylcobalamin-dependent class II (NrdJ) contains bot

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

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

122 This adenosylcobalamin-dependent enzyme is postulated to gene

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

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

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

126 Adenosylcobalamin-dependent enzymes accelerate the cleav

127 Adenosylcobalamin-dependent enzymes catalyze a variety o

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

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

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

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

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

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

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

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

136 Adenosylcobalamin-dependent glutamate mutase catalyzes a

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

138 Adenosylcobalamin-dependent isomerases catalyze carbon s

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

140 Adenosylcobalamin-dependent methylmalonyl-CoA mutase cat

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

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

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

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

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

146 The interaction of the adenosylcobalamin-dependent ribonucleoside diphosphate r

147 The adenosylcobalamin-dependent ribonucleoside triphosphate

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

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

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

151 X-H bond activation in both radical SAM and adenosylcobalamin enzymes.

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

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

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

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

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

157 Adenosylcobalamin generated by this system supported the

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

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

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

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

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

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

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

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

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

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

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

169 Tritiated adenosylcobalamin, labeled at the exchangeable position,

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

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

172 The discovery that adenosylcobalamin (or coenzyme B(12)) can act as a light

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

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

175 e findings reveal an unexpected role for the adenosylcobalamin pathway in regulating LDLR expression

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

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

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

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

180 using atomic force microscopy (AFM) and the adenosylcobalamin riboswitch aptamer domain as an exampl

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

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

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

184 Coenzyme B(12) (AdoCbl; 5'-deoxy-5'-adenosylcobalamin), the quintessential biological organo

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

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

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

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

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