ライフサイエンスコーパス: S-adenosyl-L-methionine

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

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

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

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

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

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

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

8 site in the polymerase for the methyl donor, S-adenosyl-l-methionine.

9 cubation with purified methyltransferase and S-adenosyl-L-methionine.

10 r its two substrates, hemimethylated DNA and S-adenosyl-l-methionine.

11 s, only D47N and L49A bound the co-substrate S-adenosyl-L-methionine.

12 rms an enclosed substrate-binding pocket for S-adenosyl-L-methionine.

13 -oxo-C12-acyl-carrier protein (acyl-ACP) and S-adenosyl-L-methionine.

14 r Dnmt3a, where DNA binds first, followed by S-adenosyl-l-methionine.

15 ethionine from homocysteine and precursor of S-adenosyl-l-methionine.

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

17 sferases that use the universal methyl donor S-adenosyl-l-methionine.

18 se (ACS) catalyzes the formation of ACC from S-adenosyl-L-methionine.

19 olled reaction with the preferred substrate, S-adenosyl-L-methionine.

20 unlike the human enzyme, is not activated by S-adenosyl-L-methionine.

21 e cross-linked to the methyl-donor substrate S-adenosyl-L-methionine.

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

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

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

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

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

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

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

29 p to 50-fold more tightly in the presence of S-adenosyl-L-methionine (3), suggesting that the binding

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

31 he addition of methylene groups derived from S-adenosyl-L-methionine across the double bond of oleic

32 of beta-Ala by the action of a trifunctional S-adenosyl L-methionine (Ado-Met): beta-Ala N-methyltran

33 epresents the first protein identified as an S -adenosyl-L-methionine (AdoMet)- dependent RNA m(5)C m

34 xyl methyltransferase (SAMT), which utilizes S-adenosyl-l-methionine (AdoMet or SAM) as the methyl do

35 e Michaelis constants for DNA (K(m)(CG)) and S-adenosyl-L-methionine (AdoMet) (K(m)(AdoMet)) ranged f

36 ears to contain a mixture of the substrates, S-adenosyl-L-methionine (AdoMet) and glutamine, and the

37 Initial velocity data with peptide and S-adenosyl-L-methionine (AdoMet) and product inhibition

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

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

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

41 established class of metalloenzymes that use S-adenosyl-l-methionine (AdoMet) as a source of a 5'-deo

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

43 conserved methyltransferase fold and employs S-adenosyl-l-methionine (AdoMet) as the cofactor in meth

44 CBS is activated by S-adenosyl-L-methionine (AdoMet) by inducing a conformat

45 cesses the active site of the enzyme and the S-adenosyl-l-methionine (AdoMet) cofactor by inserting i

46 e lack of catalytic competence of the enzyme.S-adenosyl-L-methionine (AdoMet) complex.

47 rate kinetic analysis using cycloartenol and S-adenosyl-l-methionine (AdoMet) generated an intersecti

48 between HhaI methyltransferase (M.HhaI) and S-adenosyl-L-methionine (AdoMet) in the presence of a no

49 S-Adenosyl-L-methionine (AdoMet) is one of Nature's most

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

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

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

53 Eighteen subclasses of S-adenosyl-l-methionine (AdoMet) radical proteins have b

54 examined the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to an arginine side cha

55 of enzymatic transfer of methyl groups from S-adenosyl-l-methionine (AdoMet) to cytosine residues in

56 te (GAA) to Asp-134 and methyl transfer from S-adenosyl-L-methionine (AdoMet) to GAA are concerted.

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

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

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

60 c enzymes which transfer a methyl group from S-adenosyl-L-methionine (AdoMet) to the amino group of e

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

62 atalyzes the transfer of a methyl group from S-adenosyl-l-methionine (AdoMet) to the N1 position of G

63 S-Adenosyl-L-methionine (AdoMet) which is biologically s

64 decreased within 1-2 min; in the presence of S-adenosyl-l-methionine (AdoMet), activity persisted for

65 g derives from the activated methyl group of S-adenosyl-L-methionine (AdoMet), affording S-adenosyl-L

66 ost methyltransferases use the methyl donor, S-adenosyl-L-methionine (AdoMet), as a cofactor.

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

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

69 and absence of the CBS allosteric regulator S-adenosyl-l-methionine (AdoMet), only C15 and C431 of h

70 ltransferase (M.RsrI) bound to the substrate S-adenosyl-l-methionine (AdoMet), the product S-adenosyl

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

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

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

74 yltransferases (N4mC MTases) are a family of S-adenosyl-L-methionine (AdoMet)-dependent MTases.

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

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

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

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

79 S-Adenosyl-l-methionine (AdoMet):arsenic(III) methyltran

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

81 ometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltra

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

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

84 l-homocysteine is a competitive inhibitor of S-adenosyl-l-methionine and a mixed inhibitor of substra

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

86 nthase from Escherichia coli in complex with S-adenosyl-L-methionine and dethiobiotin has been determ

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

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

89 were radiolabeled on-blot using [methyl-(3)H]S-adenosyl-L-methionine and recombinant PIMT.

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

91 The NMTase had an apparent K(m) of 45 microM S-adenosyl-l-methionine and substrate inhibition was obs

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

93 The analyte is incubated for 40 min with S-adenosyl-l-methionine and the commercially available e

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

95 sequential mechanism, and either substrate (S-adenosyl-l-methionine and unmethylated DNA) may be the

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

97 se large subunit methyltransferase, bound to S-adenosyl-L-methionine, and its non-reactive analogs Az

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

99 Ursodeoxycholic acid and S-adenosyl-L-methionine are the most promising treatment

100 S-Adenosyl-l-methionine:arsenic(III) methyltransferase m

101 nscription-polymerase chain reaction detects S-adenosyl-l-methionine:arsenic(III) methyltransferase m

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

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

104 ired for reactivation of the enzyme and uses S-adenosyl-L-methionine as the methyl donor.

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

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

107 A novel S-adenosyl-l-methionine:benzoic acid carboxyl methyl tra

108 emission is the result of a decrease in both S-adenosyl-l-methionine:benzoic acid carboxyl methyltran

109 of benzoic acid in the reaction catalyzed by S-adenosyl-L-methionine:benzoic acid carboxyl methyltran

110 of benzoic acid in the reaction catalyzed by S-adenosyl-L-methionine:benzoic acid carboxyl methyltran

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

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

113 critical residue within a putative conserved S-adenosyl-l-methionine-binding domain of the L protein.

114 A mutation introduced into the S-adenosyl-l-methionine-binding motif I of a myc-tagged

115 e that the two methylase activities share an S-adenosyl-l-methionine-binding site and show that, in c

116 Most important, a mutation in the S-adenosyl-l-methionine-binding site of PRMT1 substantia

117 Amino acid changes in the putative Hmt1p S-adenosyl-L-methionine-binding site were generated and

118 among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active s

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

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

121 Betaine increased hepatic S-adenosyl-L-methionine by 28 fold in the knockouts and

122 acylated acyl-carrier protein (acyl-ACP) and S-adenosyl-L-methionine by the AHL synthase enzyme.

123 ons to the energetics of binding the charged S-adenosyl-l-methionine cofactor and to catalysis.

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

125 Kinetic analysis at constant S-adenosyl-L-methionine concentration shows that represe

126 location and interactions with the cofactor S-adenosyl-l-methionine conserved.

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

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

129 S-Adenosyl-L-methionine-dependent caffeate O-methyltrans

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

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

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

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

134 he precursor phosphocholine via a three-step S-adenosyl-L-methionine-dependent methylation of phospho

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

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

137 We have identified a new type of S-adenosyl-L-methionine-dependent methyltransferase in t

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

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

140 ncludes an additional gene, tam, encoding an S-adenosyl-l-methionine-dependent methyltransferase.

141 nature sequence motifs of the major class of S-adenosyl-L-methionine-dependent methyltransferases.

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

143 ginaceae, beta-Ala betaine is synthesized by S-adenosyl-L-methionine-dependent N-methylation of beta-

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

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

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

147 S-Adenosyl-l-methionine-dependent protein arginine N-met

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

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

150 e, we describe in P. falciparum a plant-like S-adenosyl-l-methionine-dependent three-step methylation

151 c structure of the Pseudomonas denitrificans S-adenosyl-L-methionine-dependent uroporphyrinogen III m

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

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

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

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

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

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

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

159 Glycine N-methyltransferase (S-adenosyl-l-methionine: glycine methyltransferase, EC 2

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

161 inal of PIMT (residues 611-852), which binds S-adenosyl-l-methionine, interacts respectively with the

162 However, initial binding of S-adenosyl-l-methionine is preferred.

163 nd biochemical data collectively reveal that S-adenosyl-L-methionine is selectively recognized throug

164 (K(m)(pep))) were 0.9 and 1.0 microM and for S-adenosyl-L-methionine (K(m)(AdoMet)) were 1.8 and 0.6

165 ansferable methyl group is to be attached in S-adenosyl-L-methionine, lies at the opposite end of the

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

167 as a pH optimum of 7.8, an apparent K(m) for S-adenosyl-L-methionine of 18 microM, and an apparent V(

168 The transfer of a methyl group from S-adenosyl-L-methionine onto the carboxyl group of alpha

169 rst demonstration of a direct interaction of S-adenosyl-L-methionine, or its cleavage products, with

170 a are consistent with a role for ADK and the S-adenosyl-L-methionine pathway in the control of root g

171 ine biogenesis in plants and is catalyzed by S-adenosyl-L-methionine:phosphoethanolamine N-methyltran

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

173 l Medium with Earle's salt supplemented with S-adenosyl-L-methionine, putrescine, ferric pyrophosphat

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

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

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

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

178 ansfer of a total of four methyl groups from S-adenosyl-l-methionine (S-AdoMet) to two adjacent adeno

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

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

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

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

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

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

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

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

187 products are then incubated with 14C-labeled S-adenosyl-L-methionine (SAM) and dam methyltransferase

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

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

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

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

192 established class of metalloenzymes that use S-adenosyl-l-methionine (SAM) as the precursor to a high

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

209 uggesting that viperin is a putative radical S-adenosyl-l-methionine (SAM) enzyme.

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

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

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

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

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

215 positioned near the sulfonium pole of (S,S)-S-adenosyl-L-methionine (SAM) in the modeled pyridoxal p

216 dical derived from the reductive cleavage of S-adenosyl-l-methionine (SAM) initiates substrate-radica

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

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

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

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

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

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

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

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

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

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

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

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

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

230 s the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargoni

231 The enzyme catalyzes the conversion of S-adenosyl-L-methionine (SAM) to ACC.

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

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

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

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

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

237 ructure of the pyridoxal-5'-phosphate (PLP), S-adenosyl-L-methionine (SAM), and [4Fe-4S]-dependent ly

238 inomutase (LAM) utilizes a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal 5'-phosphat

239 ignificantly bind to the methyl group donor, S-adenosyl-L-methionine (SAM), it strongly increases the

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

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

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

243 ediate to the gamma-carbon of its substrate, S-adenosyl-L-methionine (SAM), to yield ACC and 5'-methy

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

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

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

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

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

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

250 methyltransferases capable of catalyzing the S-adenosyl-L-methionine (SAM)-dependent methylation of c

251 s providing powerful tools for investigating S-adenosyl-l-methionine (SAM)-dependent methylation.

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

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

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

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

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

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

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

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

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

261 omain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM).

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

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

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

265 a sequence encoding a protein homologous to S-adenosyl-L-methionine (SAM):C-24 sterol methyl transfe

266 thesize methylbenzoate from benzoic acid and S-adenosyl-l-methionine (SAM); however, they use differe

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

268 ine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of

269 A second hepatoprotective compound, S-adenosyl-L-methionine (SAMe) also not only partially p

270 S-Adenosyl-L-methionine (SAMe) exerts many key functions

271 S-adenosyl-L-methionine (SAMe) is one of the better stud

272 S-Adenosyl-L-methionine (SAMe), a metabolite present in

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

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

275 Two S-adenosyl-l-methionine substrate molecules are located

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

277 ErmC' and of its complexes with the cofactor S -adenosyl-l-methionine, the reaction product S-adenosy

278 PIMT binds S-adenosyl-l-methionine, the methyl donor for methyltran

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

280 ansferase ErmC' transfers methyl groups from S -adenosyl-l-methionine to atom N6 of an adenine base w

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

282 translational transfer of methyl groups from S-adenosyl-L-methionine to arginine residues of proteins

283 "radical SAM" enzymes use Fe4S4 clusters and S-adenosyl-L-methionine to generate organic radicals.

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

285 residues by transferring methyl groups from S-adenosyl-L-methionine to guanidino groups of arginine

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

287 a class of enzymes that use FeS clusters and S-adenosyl-L-methionine to initiate radical-dependent ch

288 its ability to transfer a methyl group from S-adenosyl-l-methionine to N(6)-methyladenine-free lambd

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

290 C5 nucleophilic replacement of the methyl of S-adenosyl-L-methionine to produce 5-methyl-6-Cys-81-S-5

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

292 talyze the transfer of the methyl group from S-adenosyl-L-methionine to the lysine epsilon-amine has

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

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

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

296 crease of hepatic apoptosis and reduction of S-adenosyl-L-methionine was detected in both types of an

297 Apparent K(m) values for S-adenosyl-l-methionine were 4.6, 3.1, and 11 mum for WT

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

299 s to the surface of EcoDam in the absence of S-adenosyl-L-methionine, which illustrates a possible in

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