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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
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
41 established class of metalloenzymes that use S-adenosyl-l-methionine (AdoMet) as a source of a 5'-deo
43 conserved methyltransferase fold and employs S-adenosyl-l-methionine (AdoMet) as the cofactor in meth
45 cesses the active site of the enzyme and the S-adenosyl-l-methionine (AdoMet) cofactor by inserting i
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
51 ch nucleophilic attack of cytosine C5 on the S-adenosyl-L-methionine (AdoMet) methyl group is concert
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
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
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
72 fX at 1.7 A and found that it belongs to the S-adenosyl-L-methionine (AdoMet)-dependent alpha/beta-kn
81 ometric assay to quantitatively characterize S-adenosyl-L-methionine (AdoMet/SAM)-dependent methyltra
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,
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
101 nscription-polymerase chain reaction detects S-adenosyl-l-methionine:arsenic(III) methyltransferase m
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
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.
115 e that the two methylase activities share an S-adenosyl-l-methionine-binding site and show that, in c
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
122 acylated acyl-carrier protein (acyl-ACP) and S-adenosyl-L-methionine by the AHL synthase enzyme.
124 structure of this enzyme in complex with the S-adenosyl-l-methionine cofactor at 1.7 A resolution con
128 we demonstrate that the pyruvoyl cofactor of S-adenosyl-L-methionine decarboxylase (AMD1) is dynamica
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
136 es demonstrated that genetic deletion of the S-adenosyl-L-methionine-dependent methyltransferase from
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-
146 on of NcsB1, unveiling that: (i) NcsB1 is an S-adenosyl-L-methionine-dependent O-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
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
158 rin complex bound with methylation cofactor, S-adenosyl-L-methionine from Pyrococcus furiosus, at 2.7
161 inal of PIMT (residues 611-852), which binds S-adenosyl-l-methionine, interacts respectively with the
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
167 as a pH optimum of 7.8, an apparent K(m) for S-adenosyl-L-methionine of 18 microM, and an apparent V(
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
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
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 (
192 established class of metalloenzymes that use S-adenosyl-l-methionine (SAM) as the precursor to a high
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
199 Lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme and, like other mem
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
206 yase activating enzyme (PFL-AE) is a radical S-adenosyl-l-methionine (SAM) enzyme that installs a cat
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
218 es is the one-electron reductive cleavage of S-adenosyl-l-methionine (SAM) into methionine and the 5'
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
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
232 ) to cytosine (Cyt) C6, methyl transfer from S-adenosyl-l-methionine (SAM) to Cyt C5, and proton abst
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
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
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
257 introduced methyl group is assembled from an S-adenosyl-L-methionine (SAM)-derived methylene fragment
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
268 ine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of
273 (including acupuncture, omega-3 fatty acids, S-adenosyl-L-methionine, St. John's wort [Hypericum perf
277 ErmC' and of its complexes with the cofactor S -adenosyl-l-methionine, the reaction product S-adenosy
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.
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
296 crease of hepatic apoptosis and reduction of S-adenosyl-L-methionine was detected in both types of an
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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