ライフサイエンスコーパス: methionine synthase

1 stream enzymes, methylmalonyl-CoA mutase and methionine synthase.

2 ethyltetrahydrofolate to tetrahydrofolate by methionine synthase.

3 uvate formate lyase, and cobalamin-dependent methionine synthase.

4 prenyltransferases and cobalamin-independent methionine synthase.

5 lavodoxin that bind flavodoxin reductase and methionine synthase.

6 ue embryos that were completely deficient in methionine synthase.

7 , transfers electrons during reactivation of methionine synthase.

8 +/- 13.7 nm for NADPH-dependent activity of methionine synthase.

9 in trafficking, and the activation domain of methionine synthase.

10 lamin-dependent enzymes glutamate mutase and methionine synthase.

11 mmalian homologues of E. coli flavodoxin and methionine synthase.

12 hway for the reductive activation of porcine methionine synthase.

13 anol-dependent methanogenesis, as well as in methionine synthase.

14 means of controlling cobalamin reactivity in methionine synthase.

15 b5 reconstitute the activity of the porcine methionine synthase.

16 flavodoxin, shuttle electrons from NADPH to methionine synthase.

17 when similar mutations were introduced into methionine synthase.

18 ge for electron transfer to the cobalamin of methionine synthase.

19 ween oxidized flavodoxin and methylcobalamin methionine synthase.

20 inding domain with methylcobalamin-dependent methionine synthase.

21 l portion of the cobalamin-binding region of methionine synthase.

22 f chaperones to a single cytoplasmic target, methionine synthase.

23 S coordination for cofactor off-loading onto methionine synthase.

24 ually and in combination in a strain lacking methionine synthase.

25 ity to reduce cytochrome c and to reactivate methionine synthase.

26 le in repairing inactive cobalamin-dependent methionine synthase.

27 h may mediate or facilitate interaction with methionine synthase.

28 ontain genes encoding MTHFR and two distinct methionine synthases.

29 ylenetetrahydrofolate reductase (1298AC/CC), methionine synthase (2756AA), and methionine synthase re

30 Human cDNAs for methionine synthase (5-methyltetrahydrofolate:L-homocyst

31 urally similar to heme and is a cofactor for methionine synthase, a key enzyme in folate metabolism.

32 olymorphisms, which result in less effective methionine synthase activation, do not appear to result

33 After 12 months, hepatic methionine synthase activity and the ratio of S-adenosyl

34 The inhibition of methionine synthase activity disrupted carbon flow throu

35 iochemical data suggested that low levels of methionine synthase activity in the first patient may re

36 It supports methionine synthase activity in the presence of NADPH an

37 NO inhibits methionine synthase activity in vitro, but data concerni

38 acid into protein, we show that NO inhibits methionine synthase activity in vivo, in cultured mammal

39 tes of cobalamin and that NO's inhibition of methionine synthase activity most likely involves its re

40 ne synthase-deficient patients have residual methionine synthase activity or that humans have a compe

41 ne-homocysteine S-methyltransferase, whereas methionine synthase activity remained diminished.

42 cobalamin demand, and management of reduced methionine synthase activity through changes in folate a

43 turbs methionine metabolism by impairment of methionine synthase activity, resulting in deoxynucleosi

44 Ethanol feeding reduced liver methionine synthase activity, S-adenosylmethionine (SAM)

45 was increased and correlated inversely with methionine synthase activity.

46 bacteria that has a dual function both as a methionine synthase and a GBT methyltransferase.

47 ino acid starvation test conditions, whereas methionine synthase and acetolactate synthase were not.

48 inactive in vivo in microbial bioassays for methionine synthase and acted as an in vitro inhibitor o

49 Studies with purified mammalian methionine synthase and cystathionine beta-synthase have

50 try catalyzed by the vitamin B(12)-dependent methionine synthase and is impaired in the cblC group of

51 l by cells of the body that have the enzymes methionine synthase and methyl malonyl CoA mutase, which

52 The recent structures of cobalamin-dependent methionine synthase and methylmalonyl-CoA mutase have re

53 Cobalamin (Cbl) is an essential cofactor for methionine synthase and methylmalonyl-CoA mutase, but it

54 idation, disabling activation of the enzymes methionine synthase and methylmalonyl-CoA mutase, disrup

55 ed for the function of the essential enzymes methionine synthase and methylmalonyl-CoA mutase, respec

56 orms that support the B12-dependent enzymes, methionine synthase and methylmalonyl-CoA mutase.

57 alamin) is an essential cofactor required by methionine synthase and methylmalonyl-CoA mutase.

58 d by the two B(12)-dependent target enzymes, methionine synthase and methylmalonyl-CoA mutase.

59 ional change on binding to the apoenzymes of methionine synthase and methylmalonyl-coenzyme A mutase:

60 ity of the 2 vitamin B-12-dependent enzymes, methionine synthase and MMA-coenzyme A mutase.

61 at this is primarily performed by the enzyme methionine synthase and only when methionine availabilit

62 ate, Cys-262, completes cofactor transfer to methionine synthase and release of a cysteine disulfide-

63 nd IDS1; S-adenosyl methionine synthase; and methionine synthase), and other cellular mechanisms (pat

64 dependent enzymes, such as the B12-dependent methionine synthase, and by enzymes involved in the bios

65 soflavone reductase-like protein, S-adenosyl methionine synthase, and cysteine synthase isoform were

66 bility to serve as a cofactor for the enzyme methionine synthase, and that aquocobalamin could quench

67 rily as a cofactor for vitamin B12-dependent methionine synthase, and that cobalamin auxotrophy has a

68 proteins IDS3a, IDS3b, and IDS1; S-adenosyl methionine synthase; and methionine synthase), and other

69 The MetH methionine synthase appears to be required for conversio

70 endent (MetE) and cobalamin-dependent (MetH) methionine synthases are two such enzyme families.

71 t for supporting NADPH-dependent activity of methionine synthase at a level that is comparable with t

72 who has an isolated functional deficiency of methionine synthase but appears to be distinct from the

73 We demonstrate that the mammalian methionine synthase can be activated in an NADPH-depende

74 Third, methionine synthase can be activated in vitro by a two-c

75 ion, they suggest directly that mutations in methionine synthase can lead to elevated homocysteine, i

76 itch from the B. subtilis yitJ gene encoding methionine synthase, can be converted into Spinach ribos

77 Methionine synthase catalyzes a methyl transfer reaction

78 Cobalamin-dependent methionine synthase catalyzes the transfer of a methyl g

79 Cobalamin-dependent methionine synthase catalyzes the transfer of a methyl g

80 Methionine synthase catalyzes the transfer of a methyl g

81 Vitamin B12-dependent methionine synthase catalyzes the transfer of a methyl g

82 ding leads to changes in the distribution of methionine synthase conformations.

83 These data suggest that genetic variation in methionine synthase could mediate risk of childhood leuk

84 The nitric-oxide-induced inactivation of methionine synthase could offer a rational explanation f

85 Human patients with methionine synthase deficiency exhibit homocysteinemia,

86 born errors resulting in isolated functional methionine synthase deficiency fall into two complementa

87 Whether any human patients with methionine synthase deficiency have a complete absence o

88 To better study the pathophysiology of methionine synthase deficiency, we utilized gene-targeti

89 development in mice and suggest either that methionine synthase-deficient patients have residual met

90 ent vitamin B12 alleviates DTT toxicity in a methionine synthase-dependent manner.

91 The association of flavodoxin and methionine synthase depends on ionic strength and pH; th

92 ember of the reductive activation system for methionine synthase describes a function for this protei

93 hat the cblG cell line has defects affecting methionine synthase directly, whereas the cblE cell line

94 s family include the vitamin B(12)-dependent methionine synthases, E. coli S-methylmethionine-S-homoc

95 bamides that were differentially utilized by methionine synthase (EC 2.1.1.13), ethanolamine ammonia-

96 homology to bacterial vitamin B12-dependent methionine synthases (EC).

97 The cobalamin-independent methionine synthase enzyme catalyzes a challenging react

98 ifts to higher energy when binding to either methionine synthase enzyme, suggesting that there is a s

99 endent (MetE) and cobalamin-dependent (MetH) methionine synthase enzymes of Escherichia coli.

100 In this paper, we offer evidence that methionine synthase exists in two different conformation

101 We found little evidence that defects in methionine synthase expression or mutations in the MS ge

102 t has only a small effect on the affinity of methionine synthase for flavodoxin.

103 tion of both O-methyltransferases (OMTs) and methionine synthase (for provision of C1 units) appears

104 Expression of methionine synthase from a plasmid containing the modifi

105 The cobalamin-independent methionine synthase from Candida albicans, known as Met6

106 Methionine synthase from E. coli catalyzes its own react

107 ructure of the cobalamin-binding fragment of methionine synthase from Escherichia coli (EC 2.1.1.13),

108 ologous to the cobalamin-binding fragment of methionine synthase from Escherichia coli and possessed

109 Cobalamin-dependent methionine synthase from Escherichia coli catalyzes the

110 Cobalamin-dependent methionine synthase from Escherichia coli is a monomeric

111 d proteogenomics reveals a B(12)-independent methionine synthase fusion protein (MetE-fusion) that is

112 vide the first evidence for mutations in the methionine synthase gene being culpable for the cblG phe

113 gene-targeting technology to inactivate the methionine synthase gene in mice.

114 The human methionine synthase gene was localized to chromosome reg

115 nsic thiol oxidase activity of the mammalian methionine synthase has been proposed to be involved.

116 onserved histidine and aspartate residues in methionine synthase have recently been described.

117 ase reductase, serves as a redox partner for methionine synthase in an NADPH-dependent reaction.

118 P1173L mutation in the activation domain of methionine synthase in the cblG cell line WG1505.

119 It is able to fully activate methionine synthase in the presence of soluble cytochrom

120 result in less efficient reductive repair of methionine synthase in vivo.

121 reduced cob(II)alamin for the activation of methionine synthase) indicates a dual physiological role

122 further evidence that NO was acting through methionine synthase inhibition.

123 ention of the cobalamin-dependent version of methionine synthase instead of the cobalamin-independent

124 Methionine synthase is a key enzyme in the methionine cy

125 Binding of methylcobalamin to full-length methionine synthase is accompanied by ligand substitutio

126 intermediate, cob(I)alamin, the activity of methionine synthase is additionally dependent on a redox

127 Methionine synthase is an essential cobalamin-dependent

128 of paramount physiological importance since methionine synthase is an essential enzyme that plays a

129 e 959 of the C-terminal activation domain of methionine synthase is assigned as its partner.

130 It has recently been shown that methionine synthase is constructed from at least four se

131 that the primary role of the ligand triad in methionine synthase is controlling the distribution of e

132 trates, products and downstream metabolites, methionine synthase is directly involved in the sulphur

133 Interestingly, we demonstrate that methionine synthase is essential for A. fumigatus virule

134 20-fold higher stoichiometry of reductase to methionine synthase is required for NR1 versus methionin

135 ; however, a 3-4-fold higher ratio of MSR to methionine synthase is required to elicit maximal activi

136 Complex formation between MMADHC and methionine synthase is signaled by loss of the lower axi

137 nzimidazole on binding of methylcobalamin to methionine synthase, is dissociated from the cobalt of t

138 The metE product, a methionine synthase, is one of the most abundant protein

139 in CNS function at all ages, especially the methionine-synthase mediated conversion of homocysteine

140 Cobalamin-independent methionine synthase (MetE) catalyzes the final step in E

141 Cobalamin-independent methionine synthase (MetE) catalyzes the final step of d

142 Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of the

143 uch that the presence of the B12-independent methionine synthase (METE) enables growth without this v

144 Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyz

145 Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyz

146 n 1 (CBA1) and the B(12)-independent form of methionine synthase (METE) were shown to regulate transg

147 ntified is the cobalamin-independent form of methionine synthase (MetE).

148 owth because it encodes a B(12) -independent methionine synthase, METE, the gene for which is suppres

149 , function of V. cholerae cobamide-dependent methionine synthase MetH was robustly supported by cobal

150 Cobalamin-dependent methionine synthase (MetH) catalyzes the methylation of

151 Cobalamin-dependent methionine synthase (MetH) catalyzes the synthesis of me

152 Methionine synthase (MetH) catalyzes the transfer of a m

153 Cobalamin-dependent methionine synthase (MetH) catalyzes the transfer of met

154 Methionine synthase (MetH) from Escherichia coli catalyz

155 B(12)-dependent methionine synthase (MetH) from Escherichia coli is a la

156 The cobalamin-dependent methionine synthase (MetH) from Escherichia coli is a mo

157 Cobalamin-dependent methionine synthase (MetH) is a 136-kDa multimodular enz

158 B(12)-dependent methionine synthase (MetH) is a large modular enzyme tha

159 Cobalamin-dependent methionine synthase (MetH) is a modular protein that cat

160 Methionine synthase (MetH) is a modular protein with at

161 Cobalamin-dependent methionine synthase (MetH) of Escherichia coli is a 136

162 Cobalamin-dependent methionine synthase (MetH) of Escherichia coli is a larg

163 amin-binding domains of either the classical methionine synthase (MetH) or the GBT methyltransferases

164 they need as a cofactor for B(12) -dependent methionine synthase (METH).

165 h is used as a cofactor in their specialized methionine synthase (MetH).

166 he reaction catalyzed by cobalamin-dependent methionine synthase (MetH, EC 2.1.1.3).

167 formin-induced longevity by mutation of worm methionine synthase (metr-1) and S-adenosylmethionine sy

168 that ubiquitously expresses a modified tRNA methionine synthase, metRS, which preferentially incorpo

169 th greatly diminished steady-state levels of methionine synthase mRNA.

170 te reductase (MTHFR 677C-->T and 1298A-->C), methionine synthase (MS 2756A-->G), and cystathionine-be

171 Polymorphisms in methionine synthase (MS A2756G), cytosolic serine hydrox

172 ed in intracellular homocysteine management, methionine synthase (MS) and cystathionine beta-synthase

173 anol feeding alone reduced the activities of methionine synthase (MS) and MATIII and increased the ac

174 Methionine synthase (MS) catalyzes methylation of homocy

175 Methionine synthase (MS) catalyzes the folate-dependent

176 Methionine synthase (MS) is a cobalamin dependent enzyme

177 Cobalamin-dependent methionine synthase (MS) is a key enzyme in methionine a

178 Methionine synthase (MS) is a key enzyme that clears int

179 The folate and vitamin B12-dependent enzyme methionine synthase (MS) is highly sensitive to cellular

180 eine, which can undergo transmethylation via methionine synthase (MS) or transsulfuration via cystath

181 Sustained activity of mammalian methionine synthase (MS) requires MS reductase (MSR), bu

182 Children with the A2756G polymorphism in methionine synthase (MS) were more likely to demonstrate

183 levels of the homocysteine junction enzymes, methionine synthase (MS), MS reductase (MSR), and cystat

184 ethylation of homocysteine, which depends on methionine synthase (MS, encoded by MTR), methionine syn

185 20T); reduced folate carrier (RFC G80A); and methionine synthase (MTR A2756G), making the present stu

186 rofolate reductase (MTHFR C677T and A1298C), methionine synthase (MTR A2756G), methionine synthase re

187 teine remethylation/methionine biosynthesis--methionine synthase (MTR) A2756G and methionine synthase

188 hylate homocysteine, vitamin B(12)-dependent methionine synthase (MTR) and betaine-homocysteine methy

189 Human methionine synthase (MTR) is a cobalamin-dependent enzym

190 etrahydrofolate reductase (MTHFR) rs1801133, methionine synthase (MTR) rs1805087 [wild-type (WT)], MT

191 methylenetetrahydrofolate reductase (MTHFR), methionine synthase (MTR), methionine synthase reductase

192 ethylene tetrahydrofolate reductase (MTHFR), methionine synthase (MTR), proton-coupled folate transpo

193 folate reductase [MTHFR] 677C>T and 1298A>C, methionine synthase [MTR] 2756A>G, cystathionine beta-sy

194 e novo dTMP biosynthesis was investigated in methionine synthase-null human fibroblast and nitrous ox

195 Methionine synthase, one of only two mammalian enzymes k

196 tabolic fates: transmethylation catalyzed by methionine synthase or betaine homocysteine methyl trans

197 e two mammalian cobalamin-dependent enzymes, methionine synthase or methylmalonyl-coenzyme A mutase;

198 ormation of a complex between flavodoxin and methionine synthase perturbs the midpoint potentials of

199 In mammals, methionine synthase plays a central role in the detoxifi

200 12 requirements is defined by the isoform of methionine synthase possessed by an alga, such that the

201 methylation of homocysteine to methionine by methionine synthase), produce more homocysteine thiolact

202 interactions between E. coli flavodoxin and methionine synthase provide a model for the mammalian sy

203 modeled as a reduction in the V(max) of the methionine synthase reaction, results in a secondary fol

204 ydrofolate and adequate vitamin B-12 for the methionine synthase reaction.

205 298AC/CC), methionine synthase (2756AA), and methionine synthase reductase (66GG).

206 Methionine synthase reductase (MSR) catalyzes the conver

207 also showed that purified recombinant human methionine synthase reductase (MSR) in combination with

208 Methionine synthase reductase (MSR) is a diflavin oxidor

209 Human methionine synthase reductase (MSR) is a protein contain

210 d A1298C), methionine synthase (MTR A2756G), methionine synthase reductase (MTRR A66G), cystathionine

211 ma cobalamin status in participants with the methionine synthase reductase (MTRR) 524CC genotype only

212 te reductase (MTHFR) 677C-->T and 1298A-->C, methionine synthase reductase (MTRR) 66A-->G, and cystat

213 thesis--methionine synthase (MTR) A2756G and methionine synthase reductase (MTRR) A66G--provided evid

214 to oxidative inactivation and is repaired by methionine synthase reductase (MTRR) in the presence of

215 Methionine synthase reductase (MTRR) is another enzyme e

216 The enzyme methionine synthase reductase (Mtrr) is necessary for ut

217 eductase (MTHFR), methionine synthase (MTR), methionine synthase reductase (MTRR), and cystathionine

218 hylenetetrahydrofolate reductase (MTHFR) and methionine synthase reductase (MTRR), have generated con

219 We investigated 5 polymorphisms in the methionine synthase reductase (MTRR), methylenetetrahydr

220 ytotoxicity was observed in cells expressing methionine synthase reductase (MTRR), novel diflavin oxi

221 tathionine beta-synthase [CBS] 844ins68, and methionine synthase reductase [MTRR] 66A>G) in 452 young

222 cloned and expressed the cDNA encoding human methionine synthase reductase and demonstrate that it is

223 and cblG classes of patients with defects in methionine synthase reductase and methionine synthase, r

224 ptophan in related diflavin reductases (e.g. methionine synthase reductase and novel reductase 1), an

225 of mutations in the gene encoding a putative methionine synthase reductase in the cblE class of patie

226 PH is 2.6 +/- 0.5 microm, and the K(act) for methionine synthase reductase is 80.7 +/- 13.7 nm for NA

227 Methionine synthase reductase is a soluble, monomeric pr

228 Methionine synthase reductase reduces cytochrome c in an

229 genes (e.g., cystathionine-beta-synthase and methionine synthase reductase).

230 s, the electron is thought to be provided by methionine synthase reductase, a protein containing a do

231 on methionine synthase (MS, encoded by MTR), methionine synthase reductase, and methylenetetrahydrofo

232 oxidoreductase with significant homology to methionine synthase reductase, NR1, has been described r

233 he soluble dual flavoprotein oxidoreductase, methionine synthase reductase, serves as a redox partner

234 thionine synthase is required for NR1 versus methionine synthase reductase, suggesting that it may re

235 e P450 reductase, nitric oxide synthase, and methionine synthase reductase.

236 ein, which is comparable with that seen with methionine synthase reductase.

237 component of the nitric-oxide synthases and methionine-synthase reductase.

238 The reactions catalyzed by methionine synthase require deprotonation of the substra

239 drial methylmalonyl-CoA mutase and cytosolic methionine synthase, respectively.

240 defects in methionine synthase reductase and methionine synthase, respectively.

241 , the binding of flavodoxin to cob(II)alamin methionine synthase results in a change in the coordinat

242 structure of the cobalamin-binding region of methionine synthase reveals that the cofactor is sandwic

243 CblD, CblC, and the activation domain of methionine synthase share several distinguishing feature

244 ts with an isolated functional deficiency of methionine synthase suggested a role for this protein in

245 zymes that require B12, gene inactivation of methionine synthase suppressed the mitochondrial fission

246 holo-MetH protein, a MetH(2-649) fragment of methionine synthase that contains the regions that bind

247 taining both FAD and FMN, and it reactivates methionine synthase that has lost activity due to oxidat

248 In methionine synthase, the best studied of the methyltrans

249 Methionine synthase, the enzyme that catalyses the trans

250 e corrin ring; when methylcobalamin binds to methionine synthase, the ligand is replaced by histidine

251 pression of metE, encoding a B12-independent methionine synthase, the other controls expression of pp

252 the conversion of the inactive form of human methionine synthase to the active state of the enzyme.

253 r relative affinities for the redox partner, methionine synthase, underlie the differences in the rel

254 the activity of the folate-dependent enzyme methionine synthase was diminished 52%.

255 Highly purified rat liver methionine synthase was inactivated in a partially irrev

256 Rat liver methionine synthase was shown to be inactivated by the n

257 residues in the cobalamin-binding region of methionine synthase, we have constructed a synthetic mod

258 ing interface between E. coli flavodoxin and methionine synthase, we have employed site-directed muta

259 Histidine 759 of methionine synthase, which replaces the normal lower lig

260 e cblG patient has greatly reduced levels of methionine synthase while in another, the enzyme is spec

261 he mutant is depleted in FMN and reactivates methionine synthase with 8% of the efficiency of wild ty

262 A model for the interaction of methionine synthase with flavodoxin is proposed in which

263 Significantly, the variants activate methionine synthase with the same V(max); however, a 3-4