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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

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