ライフサイエンスコーパス: S-adenosyl-L-homocysteine

1 cytosine ring and towards the sulfur atom of S-adenosyl-L-homocysteine.

2 A-specific m(6)A methyltransferase, bound to S-adenosyl-L-homocysteine.

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

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

5 ined at 1.89 A resolution in the presence of S-adenosyl-L-homocysteine.

6 omocysteine to give homologated analogues of S-adenosyl-L-homocysteine.

7 nsferase (hPNMT) complexed with its product, S-adenosyl-L-homocysteine (4), and the most potent inhib

8 vitro largely by increasing the formation of S-adenosyl-L-homocysteine (a potent noncompetitive inhib

9 By contrast, inclusion of 1.0 mM S-adenosyl-L-homocysteine, a potent inhibitor of catecho

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

11 In this assay, S-adenosyl-l-homocysteine (AdoHcy or SAH), a common prod

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

13 ne (AdoMet) and glutamine, and the products, S-adenosyl-L-homocysteine (AdoHcy) and N(5)-methylglutam

14 s inhibited by two products of the reaction, S-adenosyl-L-homocysteine (AdoHcy) and N,N-dimethyltrypt

15 tetrameric complex with the cofactor product S-adenosyl-l-homocysteine (AdoHcy) at 2.4 angstrom resol

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

17 of a deletion mutant of DNMT2 complexed with S-adenosyl-L-homocysteine (AdoHcy) has been determined a

18 equire a different vicinity for binding with S-adenosyl-l-homocysteine (AdoHcy) hydrolase and/or addi

19 S-Adenosyl-L-homocysteine (AdoHcy) hydrolase has been sh

20 Domain motions of S-adenosyl-l-homocysteine (AdoHcy) hydrolase have been d

21 and concentration-dependent inactivation of S-adenosyl-L-homocysteine (AdoHcy) hydrolase producing s

22 tiomers are known to be potent inhibitors of S-adenosyl-L-homocysteine (AdoHcy) hydrolase.

23 e substrates of the "hydrolytic activity" of S-adenosyl-L-homocysteine (AdoHcy) hydrolase.

24 e substrates of the "hydrolytic activity" of S-adenosyl-l-homocysteine (AdoHcy) hydrolase.

25 e and its 4'-epimer are potent inhibitors of S-adenosyl-L-homocysteine (AdoHcy) hydrolase.

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

27 dependent small molecule methyltransferases, S-adenosyl-L-homocysteine (AdoHcy) inhibited METTL7B act

28 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecula

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

30 ition sequence, and with the cofactor analog S-adenosyl-L-homocysteine (AdoHcy), has been determined.

31 -adenosyl-l-methionine (AdoMet), the product S-adenosyl-l-homocysteine (AdoHcy), the inhibitor sinefu

32 binary complex with the methyl-donor product S-adenosyl-L-homocysteine (AdoHcy).

33 ex of the enzyme, cognate DNA, and AdoMet or S-adenosyl-L-homocysteine (AdoHcy).

34 In this assay, S-adenosyl-L-homocysteine (AdoHcy/SAH), the transmethyla

35 S-adenosyl-L-methionine (AdoMet), affording S-adenosyl-L-homocysteine (AdoHcys) and a proton as the

36 unmethylated or methylated DNA together with S-adenosyl-L-homocysteine, along with the previously-sol

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

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

39 (d (min) = 1.8 angstrom), or in complex with S-adenosyl-l-homocysteine and (S)-cis-N-methylstylopine

40 lysis of a ternary complex involving M.HhaI, S-adenosyl-l-homocysteine and a double-stranded 13-mer o

41 bursaria chlorella virus 1 bound to cofactor S-adenosyl-L-homocysteine and a histone H3 peptide conta

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

43 adenosyl-L-methionine, and then the products S-adenosyl-L-homocysteine and methylated DNA are release

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

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

46 Inhibitors of methyl transfer, such as S-adenosyl-L-homocysteine and sinefungin, were shown to

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

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

49 -adenosyl-l-methionine, the reaction product S-adenosyl-l-homocysteine and the methyltransferase inhi

50 deprotonation after dissociation of AdoHcy (S-adenosyl-L-homocysteine) and before binding of AdoMet.

51 ucture of a ternary complex including DIM-5, S-adenosyl-L-homocysteine, and a substrate H3 peptide.

52 cal plots and preincubation studies revealed S-adenosyl-L-homocysteine as a competitive inhibitor to

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

54 the latter structures, SUMT has the product S-adenosyl-L-homocysteine bound in the crystal.

55 ted hamsters and increased concentrations of S-adenosyl-L-homocysteine by 5-15 nmol/g of wet tissue,

56 exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitatin

57 cture of the human enzyme containing a bound S-adenosyl-l-homocysteine cofactor is reported here at a

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

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

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

61 ionine (d (min) = 1.6 angstrom), the product S-adenosyl-l-homocysteine (d (min) = 1.8 angstrom), or i

62 S-adenosyl-L-homocysteine.DNA crystal structures.

63 The S-adenosyl-L-homocysteine exhibits an extended conformat

64 EA) is a potent inhibitor (IC(50) = 7 nm) of S-adenosyl-l-homocysteine hydrolase (AdoHcyase).

65 The crystal structure of rat liver S-adenosyl-L-homocysteine hydrolase (AdoHcyase, EC 3.3.1

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

67 The structure and fluctuations of the enzyme S-adenosyl-L-homocysteine hydrolase (SAHH) are analyzed

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

69 S-adenosyl-l-homocysteine hydrolase (SAHH) was recently

70 tion of aldosterone-induced Na+ transport by S-adenosyl-L-homocysteine hydrolase (SAHHase), the only

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

72 Iodo compound 3c appears to inactivate S-adenosyl-L-homocysteine hydrolase by a type I ("cofact

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

74 binding of these non-hydrolyzed analogues to S-adenosyl-L-homocysteine hydrolase was observed.

75 compound was originally designed to inhibit S-adenosyl-L-homocysteine hydrolase, it has been found t

76 te with type I mechanism-based inhibition of S-adenosyl-L-homocysteine hydrolase.

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

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

79 inhibition studies with SUV39H1 showed that S-adenosyl-l-homocysteine is a competitive inhibitor of

80 rase (BAMT) activity and the ratio of SAM to S-adenosyl-l-homocysteine ("methylation index") after po

81 S-Adenosyl-L-homocysteine, produced by the methylation o

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

83 relationship between isoaspartate levels and S-adenosyl-l-homocysteine production was found to be lin

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

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

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

87 4'-O-methyltransferase RebM in complex with S-adenosyl-l-homocysteine revealed RebM to adopt a typic

88 salicylic acid and the demethylated product S-adenosyl-L-homocysteine reveals a protein structure th

89 -A crystal structure of COMT in complex with S-adenosyl-L-homocysteine (SAH) and ferulic acid (ferula

90 Besides the natural inhibitors S-adenosyl-l-homocysteine (SAH) and sinefungin (SFG), we

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

92 ter and l-alanine in place of l-lysine, with S-adenosyl-l-homocysteine (SAH) bound to the cluster in

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

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

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

96 ly enzyme in vertebrates known to catabolize S-adenosyl-L-homocysteine (SAH), an end product inhibito

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

98 Fe-4S](2+/1+) couple in the presence of SAM, S-adenosyl-l-homocysteine (SAH), or 5'-{N-[(3S)-3-aminoc

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

100 FR bound to SAM and its demethylated product S-adenosyl-L-homocysteine (SAH).

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

102 value and is weakly inhibited by the product S-adenosyl-l-homocysteine (SAH).

103 ism and the flux of S-adenosyl methionine to S-adenosyl-L-homocysteine (SAM-to-SAH), thereby, modulat

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

105 und to cognate DNA and the cofactor analogue S-adenosyl-l-homocysteine shows an increase in cavity vo

106 on of catecholestrogens is inhibited more by S-adenosyl-L-homocysteine than by quercetin.

107 ites results in stoichiometric production of S-adenosyl-l-homocysteine that is separated from the oth

108 e specific by competition with low levels of S-adenosyl-L-homocysteine, the product of methyl-group t

109 MeT1 in complex with its exhausted cofactor, S-adenosyl-l-homocysteine, together with mutagenesis stu

110 (AdoMet) and product inhibition studies with S-adenosyl-L-homocysteine were performed to assess the k

111 The sulfur atom of S-adenosyl-L-homocysteine, where the transferable methyl

112 ly potent methylation-specific inhibitor was S-adenosyl-L-homocysteine, which also displayed a comple