ライフサイエンスコーパス: S-adenosyl

1 poenzyme, PaMTH1-SAM (co-factor), and PaMTH1-S-adenosyl homocysteine (by-product) co-complexes refine

2 romatography/mass spectrometry (LC/MS)-based S-adenosyl homocysteine (SAH) detection assay for histon

3 Here, we describe a suite of S-adenosyl homocysteine (SAH) photoreactive probes and t

4 ethyltransferase mechanisms, the addition of S-adenosyl homocysteine (SAH), which is the by-product a

5 in the free form and a ternary complex with S-adenosyl homocysteine and a histone H3 peptide and bio

6 ed the expression of DNMT1, MMP9, TIMP1, and S-adenosyl homocysteine hydrolase (SAHH) and upregulated

7 We show here that the cofactor analogue S-adenosyl homocysteine promotes this promiscuous DNA cl

8 .01), and the decreased S-adenosylmethionine/S-adenosyl homocysteine ratio (P<0.01).

9 when PIMT protein binding was poisoned with S-adenosyl homocysteine.

10 ence and absence of its methyl donor product S-adenosyl-homocysteine (SAH) and its ortholog scTrm10 f

11 ibility possibly reflected in high levels of S-adenosyl-homocysteine (SAH) and low levels of S-adenos

12 (SAM), which is converted via methylation to S-adenosyl-homocysteine (SAH), which accumulates during

13 d that 1 equiv each of 5'-deoxyadenosine and S-adenosyl-homocysteine are produced for each methylatio

14 Inhibition studies on S-adenosyl-homocysteine, thioadenosine, methylthioadenos

15 chaelis-Menten kinetics, and is inhibited by S-adenosyl-homocysteine.

16 The S-adenosyl- l-homocysteine (AdoHcy) hydrolases (SAHH) fr

17 e TPMT, as a binary complex with the product S-adenosyl- l-homocysteine and as a ternary complex with

18 l-homocysteine and as a ternary complex with S-adenosyl- l-homocysteine and the substrate 6-mercaptop

19 rine by methylating them in a reaction using S-adenosyl- l-methionine as the donor.

20 that is generated by a reductive cleavage of S-adenosyl- l-methionine.

21 ses K m for 6-mercaptopurine but not K m for S-adenosyl- l-methionine.

22 ibitors and immunoprecipitation of RyR2 from S-adenosyl-l-[methyl-(3)H]methionine ([(3)H]SAM) pretrea

23 d from yeast cells radiolabeled in vivo with S-adenosyl-l-[methyl-(3)H]methionine.

24 l analysis of Rpl3 radiolabeled in vivo with S-adenosyl-l-[methyl-(3)H]methionine.

25 and reductant and then incubated with excess S-adenosyl-l-[methyl-d3]methionine in the presence of su

26 ere determined for MycE bound to the product S-adenosyl-L-homocysteine (AdoHcy) and magnesium, both w

27 TbPRMT7 in complex with its cofactor product S-adenosyl-l-homocysteine (AdoHcy) at 2.8 A resolution a

28 The S-adenosyl-l-homocysteine (AdoHcy) hydrolases catalyze t

29 ne hydrolase (AHCY) hydrolyzes its substrate S-adenosyl-L-homocysteine (AdoHcy) to L-homocysteine (Hc

30 ures of human NTMT1 in complex with cofactor S-adenosyl-L-homocysteine (SAH) and six substrate peptid

31 The affinity of S-adenosyl-l-homocysteine (SAH) for SAM binding proteins

32 ive and sensitive fluorescent biosensors for S-adenosyl-l-homocysteine (SAH) that provide a direct "m

33 SAHH) catalyzes the reversible conversion of S-adenosyl-L-homocysteine (SAH) to adenosine (ADO) and L

34 e product of the methyltransferase reaction, S-adenosyl-l-homocysteine (SAH), is converted into adeni

35 equence (5'-(m7)G0pppA1G2U3U4G5U6U7-3'), and S-adenosyl-l-homocysteine (SAH), the by-product of the m

36 ne and the second SAM (SAM2) is converted to S-adenosyl-l-homocysteine (SAH).

37 otein alpha-amine, resulting in formation of S-adenosyl-l-homocysteine and alpha-N-methylated protein

38 syl-l-methionine (AdoMet) to glycine to form S-adenosyl-l-homocysteine and sarcosine.

39 ormational state complexed with the products S-adenosyl-L-homocysteine and sinapaldehyde.

40 for the malonyl moiety and was inhibited by S-adenosyl-L-homocysteine and sinefungin.

41 e, with concomitant exchanges of the product S-adenosyl-l-homocysteine and the methyl donor substrate

42 (hDNMT1, residues 351-1600) in complex with S-adenosyl-l-homocysteine at 2.62A resolution.

43 r-associated inhibiting H3K27M peptide and a S-adenosyl-l-homocysteine cofactor.

44 ransition in the active site relative to the S-adenosyl-L-homocysteine complexes, suggesting a mechan

45 tures with bound S-adenosyl-L-methionine and S-adenosyl-L-homocysteine confirm that the cofactor bind

46 S-Adenosyl-L-homocysteine hydrolase (AHCY) hydrolyzes it

47 S-Adenosyl-L-homocysteine hydrolase (SAHH) catalyzes the

48 osophila homologs of the SAH hydrolase Ahcy (S-adenosyl-L-homocysteine hydrolase [SAHH[), CG9977/dAhc

49 methylation inhibition by a novel reversible S-adenosyl-l-homocysteine hydrolase inhibitor leads to i

50 eranyl S-thiolodiphosphate (GSPP) along with S-adenosyl-L-homocysteine in the cofactor binding site,

51 se-linked continuous assay that converts the S-adenosyl-L-homocysteine product of DNA methylation to

52 DnrK-Ser in complex with aclacinomycin T and S-adenosyl-L-homocysteine refined to 1.9-A resolution re

53 S-Adenosyl-L-homocysteine remains bound in the active si

54 ture of (s-s)MetH(CT) with cob(II)alamin and S-adenosyl-L-homocysteine represents the enzyme in the r

55 4'-O-methyltransferase RebM in complex with S-adenosyl-l-homocysteine revealed RebM to adopt a typic

56 omplex with human tRNA3(Lys) and the product S-adenosyl-L-homocysteine show a dimer of heterodimers i

57 ture of the ZIKV NS5 protein in complex with S-adenosyl-L-homocysteine, in which the tandem methyltra

58 y complex with its desmethylated cosubstrate S-adenosyl-l-homocysteine.

59 eotide small RNA duplex and cofactor product S-adenosyl-l-homocysteine.

60 In this assay, S-adenosyl-l-homocystine (AdoHcy/SAH), the by-product of

61 Consistent with its effect on the predicted S-adenosyl-l-Met binding site, dim1A plants lack the two

62 Here, 4-azidobut-2-enyl derivative of S-adenosyl-L-methionine (Ab-SAM) was reported as a suita

63 Recombinant TrmO employs S-adenosyl-L-methionine (AdoMet) as a methyl donor to me

64 --> m(7)GpppA-RNA --> m(7)GpppAm-RNA), using S-adenosyl-l-methionine (AdoMet) as a methyl donor.

65 Most of these MTases use the cofactor S-adenosyl-l-Methionine (AdoMet) as a methyl source.

66 TrmD enzymes are known to use S-adenosyl-l-methionine (AdoMet) as substrate; we have s

67 The biological methyl donor S-adenosyl-l-methionine (AdoMet) is spontaneously degrad

68 ch nucleophilic attack of cytosine C5 on the S-adenosyl-L-methionine (AdoMet) methyl group is concert

69 ogenase from Bacillus circulans (BtrN) is an S-adenosyl-l-methionine (AdoMet) radical enzyme.

70 he substrate, catalyzes methyl transfer from S-adenosyl-l-methionine (AdoMet) to glycine to form S-ad

71 Mammalian CBS is modulated by the binding of S-adenosyl-l-methionine (AdoMet) to its regulatory domai

72 catalyze the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the 5-position of cy

73 may transfer one to three methyl groups from S-adenosyl-L-methionine (AdoMet) to the epsilon-amino gr

74 DNA substrate and the methyl donor cofactor, S-adenosyl-l-methionine (AdoMet), displayed AdoMet non-c

75 eductive cleavage of the sulfonium center of S-adenosyl-L-methionine (AdoMet), generating methionine

76 For example, how both the methyl donor S-adenosyl-l-methionine (AdoMet), which is water-soluble

77 fX at 1.7 A and found that it belongs to the S-adenosyl-L-methionine (AdoMet)-dependent alpha/beta-kn

78 Modification of protein residues by S-adenosyl-L-methionine (AdoMet)-dependent methyltransfe

79 S-adenosyl-L-methionine (AdoMet)-dependent O-methyltrans

80 m reduced flavodoxin and a methyl group from S-adenosyl-L-methionine (AdoMet).

81 s: homocysteine, methyltetrahydrofolate, and S-adenosyl-l-methionine (AdoMet).

82 n and a regulatory C-terminal domain binding S-adenosyl-l-methionine (AdoMet).

83 ped an enzyme-coupled luminescence assay for S-adenosyl-l-methionine (AdoMet/SAM)-based PMTs.

84 We describe a new metabolite, carboxy-S-adenosyl-l-methionine (Cx-SAM), its biosynthetic pathw

85 composed of enzymes that reductively cleave S-adenosyl-l-methionine (SAM or AdoMet) to generate a 5'

86 cts and is catalyzed by multiple families of S-adenosyl-L-methionine (SAM or AdoMet)-dependent methyl

87 S-adenosyl-L-methionine (SAM) acts as a signal and binds

88 ach, specific PMTs are engineered to process S-adenosyl-L-methionine (SAM) analogs as cofactor surrog

89 activity of vSET in vivo with an engineered S-adenosyl-l-methionine (SAM) analogue as methyl donor c

90 The synthesis of an azide-bearing N-mustard S-adenosyl-L-methionine (SAM) analogue, 8-azido-5'-(diam

91 chemoenzymatic platform for the synthesis of S-adenosyl-L-methionine (SAM) analogues compatible with

92 h of CliEn-seq involves in vivo synthesis of S-adenosyl-L-methionine (SAM) analogues from cell-permea

93 tor IIIB) domain and some of them presenting S-adenosyl-l-methionine (SAM) and nuclear receptor box (

94 NSD2 binds to S-adenosyl-l-methionine (SAM) and nucleosome substrates

95 conventional methyltransferases that utilize S-adenosyl-L-methionine (SAM) as a cofactor.

96 A-->m(7)GpppA-RNA-->m(7)GpppAm-RNA, by using S-adenosyl-l-methionine (SAM) as a methyl donor.

97 Molecular modeling and competitive S-adenosyl-l-methionine (SAM) binding assay suggest that

98 spectroscopy on the resting oxidized and the S-adenosyl-l-methionine (SAM) bound forms of pyruvate fo

99 kcat value in the conversion of 5'-ClDA into S-adenosyl-l-methionine (SAM) but a reduced kcat value i

100 route to biodiesel produces FAMEs by direct S-adenosyl-L-methionine (SAM) dependent methylation of f

101 rin-2 in a chemical reaction catalysed by an S-adenosyl-L-methionine (SAM) dependent Methyltransferas

102 S-adenosyl-l-methionine (SAM) dependent O-methyltransfer

103 Lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme and, like other mem

104 DesII, a radical S-adenosyl-l-methionine (SAM) enzyme from Streptomyces v

105 patients have mutations in MOCS1A, a radical S-adenosyl-l-methionine (SAM) enzyme involved in the con

106 Here we demonstrate that a putative radical S-adenosyl-L-methionine (SAM) enzyme superfamily member

107 d by DesII, which is a member of the radical S-adenosyl-L-methionine (SAM) enzyme superfamily.

108 DesII is a radical S-adenosyl-l-methionine (SAM) enzyme that can act as a d

109 Tryptophan lyase (NosL) is a radical S-adenosyl-l-methionine (SAM) enzyme that catalyzes the

110 yase activating enzyme (PFL-AE) is a radical S-adenosyl-l-methionine (SAM) enzyme that installs a cat

111 Viperin is predicted to be a radical S-adenosyl-l-methionine (SAM) enzyme, but it is unknown

112 SPL is a radical S-adenosyl-l-methionine (SAM) enzyme, which uses a [4Fe-

113 Radical S-adenosyl-l-methionine (SAM) enzymes are widely distrib

114 The radical S-adenosyl-L-methionine (SAM) enzymes RlmN and Cfr methy

115 Radical S-adenosyl-L-methionine (SAM) enzymes use an iron-sulfur

116 que to a family of proteins known as radical S-adenosyl-l-methionine (SAM) enzymes.

117 nding isotope effects (BIEs) of the cofactor S-adenosyl-l-methionine (SAM) for SET8-catalyzed H4K20 m

118 ransferases (MATs) catalyze the formation of S-adenosyl-l-methionine (SAM) inside living cells.

119 es is the one-electron reductive cleavage of S-adenosyl-l-methionine (SAM) into methionine and the 5'

120 S-adenosyl-L-methionine (SAM) is converted to 5'-chloro-

121 S-Adenosyl-l-methionine (SAM) is recognized as an import

122 S-adenosyl-L-methionine (SAM) is the sole methyl-donor c

123 The radical S-adenosyl-L-methionine (SAM) methyl synthases, RlmN and

124 Many cobalamin (Cbl)-dependent radical S-adenosyl-l-methionine (SAM) methyltransferases have be

125 These results indicate that the radical S-adenosyl-L-methionine (SAM) protein PylB mediates a ly

126 ts of bciD, which encodes a putative radical S-adenosyl-l-methionine (SAM) protein, are unable to syn

127 if that occurs upstream of genes involved in S-adenosyl-L-methionine (SAM) recycling in many Gram-pos

128 dent enzymes that are members of the radical S-adenosyl-l-methionine (SAM) superfamily was previously

129 QueE is a member of the radical S-adenosyl-l-methionine (SAM) superfamily, all of which

130 ranslational riboswitches were identified in S-adenosyl-l-methionine (SAM) synthetase metK genes in m

131 ) to cytosine (Cyt) C6, methyl transfer from S-adenosyl-l-methionine (SAM) to Cyt C5, and proton abst

132 erate a 3-amino-3-carboxypropyl radical from S-adenosyl-L-methionine (SAM) to form a C-C bond.

133 three cysteines in a CX(3)CX(2)C motif, and S-adenosyl-L-methionine (SAM) to generate a 5'-deoxyaden

134 hesis is the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to magnesium protoporphyri

135 er of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue o

136 es a DNA cofactor in order to stably bind to S-adenosyl-l-methionine (SAM), suggesting that it procee

137 resolution showed a single binding site for S-adenosyl-L-methionine (SAM), the methyl donor.

138 S-Adenosyl-l-methionine (SAM), the primary methyl group

139 methionine, a precursor for the synthesis of S-adenosyl-l-methionine (SAM), which is the most commonl

140 The highly conserved S-adenosyl-l-methionine (SAM)-binding residues of the Dx

141 on structures of Bud23-Trm112 in the apo and S-adenosyl-L-methionine (SAM)-bound forms.

142 Here we report a versatile S-adenosyl-l-methionine (SAM)-dependent enzyme, LepI, th

143 revealing new metalloenzymes, flavoenzymes, S-adenosyl-L-methionine (SAM)-dependent enzymes and othe

144 synthesis protein NifB catalyzes the radical S-adenosyl-L-methionine (SAM)-dependent insertion of car

145 atic analyses predicted EftM to be a Class I S-adenosyl-l-methionine (SAM)-dependent methyltransferas

146 ergent enzyme evolution has been observed in S-adenosyl-L-methionine (SAM)-dependent methyltransferas

147 rmed by O-methyltransferases, members of the S-adenosyl-l-methionine (SAM)-dependent O-methyltransfer

148 proposed to comprise two distinct groups of S-adenosyl-l-methionine (SAM)-dependent RNA enzymes, nam

149 delta position of the piperazyl scaffold is S-adenosyl-l-methionine (SAM)-dependent.

150 introduced methyl group is assembled from an S-adenosyl-L-methionine (SAM)-derived methylene fragment

151 o influence accumulation of the methyl donor S-adenosyl-L-methionine (SAM).

152 ven known families of riboswitches that bind S-adenosyl-l-methionine (SAM).

153 due and the 3-amino-3-carboxypropyl group of S-adenosyl-l-methionine (SAM).

154 tilis yitJ S-box (SAM-I) riboswitch bound to S-adenosyl-L-methionine (SAM).

155 ue, the highly abundant methylation cofactor S-adenosyl-l-methionine (SAM).

156 co-substrate for methyltransferase activity, S-adenosyl-l-methionine (SAM).

157 Sinefungin (SIN), a natural S-adenosyl-L-methionine analog produced by Streptomyces

158 es share a binding site for the methyl donor S-adenosyl-l-methionine and are inhibited by individual

159 acyl-homoserine lactones (AHL) signals using S-adenosyl-l-methionine and either cellular acyl carrier

160 lfonic acid (2-AP-6-SO3H) upon reaction with S-adenosyl-L-methionine and irradiation with UVA light,

161 Two structures with bound S-adenosyl-L-methionine and S-adenosyl-L-homocysteine co

162 verted into a succinimide on incubation with S-adenosyl-l-methionine and the commercially available e

163 inhibitors, by mimicking each substrate, the S-adenosyl-l-methionine and the deoxycytidine, and linki

164 ting many methyltransferase enzymes that use S-adenosyl-l-methionine as a cofactor.

165 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct

166 es and shed light on the structural basis of S-adenosyl-L-methionine binding and methyltransferase ac

167 -alone adenylation domain interrupted by the S-adenosyl-l-methionine binding region of a methyltransf

168 al ligands, including the first structure of S-adenosyl-l-methionine bound to a KsgA/Dim1 enzyme in a

169 structure of this enzyme in complex with the S-adenosyl-l-methionine cofactor at 1.7 A resolution con

170 we demonstrate that the pyruvoyl cofactor of S-adenosyl-L-methionine decarboxylase (AMD1) is dynamica

171 The radical S-adenosyl-L-methionine enzyme DesII from Streptomyces v

172 The radical S-adenosyl-L-methionine enzyme HydG lyses free tyrosine

173 Here we show that PhnJ is a novel radical S-adenosyl-L-methionine enzyme that catalyses C-P bond c

174 Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assemb

175 HydG is a member of the radical S-adenosyl-L-methionine family of enzymes that transform

176 rin complex bound with methylation cofactor, S-adenosyl-L-methionine from Pyrococcus furiosus, at 2.7

177 The radical S-adenosyl-l-methionine HydG, the best characterized of

178 However, only one S-adenosyl-L-methionine molecule and one substrate molec

179 approach designed to target specifically the S-adenosyl-l-methionine pocket of catechol O-methyl tran

180 enases to provide the substrates of LipA, an S-adenosyl-L-methionine radical enzyme that inserts two

181 Numerous cellular processes involving S-adenosyl-l-methionine result in the formation of the t

182 The response to S-adenosyl-L-methionine stimulation or thermal activatio

183 a far better acceptor of methyl groups from S-adenosyl-L-methionine than was malonyl-CoA.

184 ofiles of PsACS [encode enzymes that convert S-adenosyl-L-methionine to 1-aminocyclopropane-1-carboxy

185 (S)G in DNA can be methylated by S-adenosyl-l-methionine to give S(6)-methylthioguanine (

186 vates HA by transferring a methyl group from S-adenosyl-l-methionine to HA, and is the only well-know

187 specifically transfers the methyl group from S-adenosyl-L-methionine to O-4 of alpha-D-glucopyranosyl

188 ylic acid (ACC) synthases (ACS) that convert S-adenosyl-l-methionine to the immediate precursor ACC.

189 atalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the N6 position of an adenine

190 es the transfer of the methyl group from the S-adenosyl-l-methionine to the protein alpha-amine, resu

191 transferase belongs to the diverse family of S-adenosyl-l-methionine transferases.

192 otope effects.(36)S-labeled l-methionine and S-adenosyl-l-methionine were synthesized from elemental

193 Posttranslational methylation by S-adenosyl-L-methionine(SAM)-dependent methyltransferase

194 d only compete with the enzyme cofactor SAM (S-adenosyl-L-methionine) but not the substrate nucleosom

195 om Streptomyces venezuelae is a radical SAM (S-adenosyl-l-methionine) enzyme that catalyzes the deami

196 adding excess substrate for DNA methylation (S-adenosyl-L-methionine) rescues the suppression of mEPS

197 ltransferase catalytic tetrad, interact with S-adenosyl-l-methionine, and contribute to autoguanylati

198 from a solution of MoaA incubated with GTP, S-adenosyl-L-methionine, and sodium dithionite in the ab

199 ite, resulting from in situ demethylation of S-adenosyl-L-methionine, at 2.05 or 1.82 A resolution, r

200 ing the methylation site, in the presence of S-adenosyl-L-methionine, reveals a V-like protein struct

201 (including acupuncture, omega-3 fatty acids, S-adenosyl-L-methionine, St. John's wort [Hypericum perf

202 virtue of the strong electrophilic nature of S-adenosyl-l-methionine, the transmethylation of the dem

203 requires a redox-active [4Fe-4S]-cluster and S-adenosyl-L-methionine, which is reductively cleaved to

204 S-adenosyl-L-methionine- (AdoMet-) dependent methyltrans

205 The role of Glu119 in S-adenosyl-L-methionine-dependent DNA methyltransferase

206 M.EcoRI, a bacterial sequence-specific S-adenosyl-L-methionine-dependent DNA methyltransferase,

207 NfuA, and the methylthiolase MiaB, a radical S-adenosyl-L-methionine-dependent enzyme involved in the

208 e methyltransferases (MTs) that catalyze the S-adenosyl-L-methionine-dependent methylation of natural

209 RsmC is a class I S-adenosyl-L-methionine-dependent methyltransferase comp

210 es demonstrated that genetic deletion of the S-adenosyl-L-methionine-dependent methyltransferase from

211 The S-adenosyl-L-methionine-dependent methyltransferase KsgA

212 We characterized Rv0560c as an S-adenosyl-L-methionine-dependent methyltransferase that

213 acterization of a C. roseus cDNA encoding an S-adenosyl-L-methionine-dependent N methyltransferase th

214 Data from time course experiments and S-adenosyl-l-methionine-dependent O-methyltransferase in

215 NovP is an S-adenosyl-l-methionine-dependent O-methyltransferase th

216 on of NcsB1, unveiling that: (i) NcsB1 is an S-adenosyl-L-methionine-dependent O-methyltransferase; (

217 A conserved S-adenosyl-l-methionine-dependent RNA methyltransferase,

218 and in vitro enzyme studies identified a new S-adenosyl-l-methionine-dependent S-MT (TmtA) that is, s

219 cofactors, heme, pyridoxal-5'-phosphate, and S-adenosyl-l-methionine.

220 ely molecular mechanism of CBS activation by S-adenosyl-l-methionine.

221 ith (2.1 A) and without (2.0 A) its cofactor S-adenosyl-L-methionine.

222 t exchange with a fresh molecule of cofactor S-adenosyl-L-methionine.

223 e-5-phosphate and methane in the presence of S-adenosyl-L-methionine.

224 ethylthioguanine (S(6)mG) in the presence of S-adenosyl-l-methionine.

225 -homocysteine and the methyl donor substrate S-adenosyl-l-methionine.

226 his function or for allosteric regulation by S-adenosyl-L-methionine.

227 still responded to allosteric activation by S-adenosyl-L-methionine.

228 n and do not disrupt binding of the cofactor S-adenosyl-L-methionine.

229 is transfers a methyl group originating from S-adenosyl-l-methionine.

230 hylation of H3K36 using specifically labeled S-adenosyl-l-methionine.

231 ied in the TPsiC-loop of tRNA, from cofactor S-adenosyl-L-methionine.

232 xogenous application of ethylene precursors, S-adenosyl-Met and 1-aminocyclopropane-1-carboxylic acid

233 in length and targets mRNAs encoding several S-adenosyl-Met-dependent carboxyl methyltransferase fami

234 sition adjacent to the tRNA anticodon, using S-adenosyl methionine (AdoMet) as the methyl donor.

235 t catalyze transfer of the methyl group from S-adenosyl methionine (AdoMet) to the N1 position of G37

236 on of genes involved in aromatic amino acid, S-adenosyl methionine (SAM) and folate biosynthetic path

237 ) Colorado strains carrying mutations in the S-adenosyl methionine (SAM) binding site in the CR VI of

238 inistration of the (endogenous) methyl donor S-adenosyl methionine (SAM) did not affect CpG methylati

239 g the assembly of the H cluster, the radical S-adenosyl methionine (SAM) enzyme HydG lyses the substr

240 Additionally, we find that the cofactor S-adenosyl methionine (SAM) is necessary for stable inte

241 e deprivation, and that supplementation with S-adenosyl methionine (SAM) prevents both the increase i

242 NifB utilizes two equivalents of S-adenosyl methionine (SAM) to insert a carbide atom and

243 te binding cleft and lacks a properly formed S-adenosyl methionine (SAM)-binding pocket necessary for

244 S-Adenosyl methionine (SAM)-dependent C-methyltransferas

245 biomolecules by a large and diverse class of S-adenosyl methionine (SAM)-dependent methyltransferases

246 zyme A 3-O-methyltransferase (CCoAOMT) is an S-adenosyl methionine (SAM)-dependent O-methyltransferas

247 Here, we explore the mechanism for tuning of S-adenosyl methionine (SAM)-I riboswitch folding.

248 ional switching, we constructed models of an S-adenosyl methionine (SAM)-I riboswitch RNA segment inc

249 the by-product and competitive inhibitor of S-adenosyl methionine (SAM)-mediated methyltransferase r

250 t catalyze the formation of the methyl donor S-adenosyl methionine (SAM).

251 to methionine, which is in turn converted to S-adenosyl methionine (SAM; the major methyl donor).

252 S-adenosyl methionine (SAMe) improves interferon signali

253 Hepatic S-adenosyl methionine (SAMe) levels decrease in methioni

254 The use of S-adenosyl methionine (SAMe), a naturally occurring mole

255 sugars, and other small molecules, including S-adenosyl methionine and glutathione, through top-down

256 his conversion involves methyl transfer from S-adenosyl methionine and is critical to minimize tRNA f

257 In the absence of the methyl donor S-adenosyl methionine and under certain permissive react

258 L synthesis requires unique enzymes that use S-adenosyl methionine as an acyl acceptor and amino acid

259 ex with its histone H4 peptide substrate and S-adenosyl methionine cofactor.

260 with lysidine, those derived using modified S-adenosyl methionine derivatives and those using TET/JB

261 demonstrated by detecting the human radical S-adenosyl methionine domain containing 2 (RSAD2) gene,

262 and enhanced expression of the IRGs, radical S-adenosyl methionine domain containing 2 and myxovirus

263 nsfected cell lines showed that the internal S-adenosyl methionine domains of viperin were essential

264 MTase) that accept analogues of the cofactor S-adenosyl methionine have been widely deployed for alky

265 thase activity through changes in folate and S-adenosyl methionine metabolism.

266 Serine starvation increased the methionine/S-adenosyl methionine ratio, decreasing the transfer of

267 m enzymes stearoyl-CoA-desaturases (SCD) and S-adenosyl methionine synthetase (sams-1) activates the

268 We show that the MccD enzyme uses S-adenosyl methionine to transfer 3-amino-3-carboxypropy

269 that use different cofactors, primarily SAM (S-adenosyl methionine), NAD (nicotinamide adenine dinucl

270 the recruitment of the methyl donor, AdoMet (S-adenosyl methionine), to RNMT.

271 hich is required for efficient production of S-adenosyl methionine, an essential methyltransferase co

272 with Fe(2+), S(2-), MoO4(2-), R-homocitrate, S-adenosyl methionine, and Mg-ATP, is sufficient for the

273 odifying the Npl4 zinc finger domain through S-adenosyl methionine-dependent cysteine methylation.

274 methyltransferases (TMTs) might resemble the S-adenosyl methionine-dependent enzymes described for me

275 The third largest dsRNA encodes an S-adenosyl methionine-dependent methyltransferase cappin

276 hich is known to lead to increased levels of S-adenosyl methionine-the key methyl donor for DNA methy

277 dium with a mixture of labeled and unlabeled S-adenosyl methionine.

278 onstitution of TbtI, the responsible radical S-adenosyl-methionine (rSAM) C-methyltransferase, which

279 we describe the structures of RlmH bound to S-adenosyl-methionine (SAM) and the methyltransferase in

280 Antimorphic mutants in S-adenosyl-methionine (SAM) synthetase genes also induce

281 Methionine generates the methyl donor S-adenosyl-methionine (SAM), which is converted via meth

282 denosyl-homocysteine (SAH) and low levels of S-adenosyl-methionine (SAM).

283 es are critical for catalysis and binding to S-adenosyl-methionine and phosphoethanolamine substrates

284 Using S-adenosyl-methionine as the methyl donor, caffeic acid

285 se mutations, we determined the apo-form and S-adenosyl-methionine binary complex SbCOMT crystal stru

286 of NtMTHFR did not affect the methionine and S-adenosyl-methionine levels in the knockdown lines.

287 th the H3K9 methyltransferase Clr4 in a SAM (S-adenosyl-methionine)-dependent manner, and Clr4 is tra

288 ine, which is then used for the synthesis of S-adenosyl-methionine, a universal methyl donor for nume

289 ociated with the methyl cycle that generates S-adenosyl-methionine, an essential methyltransferase co

290 ek and then placebo for 2 weeks, 65 received S-adenosyl-methionine, and 34 received no specific treat

291 ptive donor substrate of glycan methylation, S-adenosyl-methionine, from the cytoplasm to the Golgi w

292 treatment with the EZH2 inhibitor, selective S-adenosyl-methionine-competitive small-molecule (GSK126

293 ate that GSK126, a potent, highly selective, S-adenosyl-methionine-competitive, small-molecule inhibi

294 tification of two previously uncharacterized S-adenosyl-methionine-dependent O-methyltransferase gene

295 xanthine phosphoribosyltransferase, and the S-adenosyl-methionine-I riboswitch from the B. subtilis

296 ulans with various assays, including in vivo S-adenosyl-[methyl-(3)H]methionine labeling, targeted in

297 ted with S-adenosyl-[methyl-3H]methionine or S-adenosyl-[methyl-14C]methionine stimulates the labelin

298 dition to mouse heart cytosol incubated with S-adenosyl-[methyl-3H]methionine or S-adenosyl-[methyl-1

299 s in enhanced transfer of methyl groups from S-adenosyl-[methyl-3H]methionine to proteins.

300 ytic subunit of the heterodimeric methionine S-adenosyl transferase-2 (MAT2A) with fluorinated N,N-di