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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

81 4'-O-methyltransferase RebM in complex with S-adenosyl-l-homocysteine revealed RebM to adopt a typic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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