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1 ethyltetrahydrofolate to tetrahydrofolate by methionine synthase.
2 uvate formate lyase, and cobalamin-dependent methionine synthase.
3 prenyltransferases and cobalamin-independent methionine synthase.
4 lavodoxin that bind flavodoxin reductase and methionine synthase.
5 ue embryos that were completely deficient in methionine synthase.
6 , transfers electrons during reactivation of methionine synthase.
7 +/- 13.7 nm for NADPH-dependent activity of methionine synthase.
8 lamin-dependent enzymes glutamate mutase and methionine synthase.
9 mmalian homologues of E. coli flavodoxin and methionine synthase.
10 hway for the reductive activation of porcine methionine synthase.
11 anol-dependent methanogenesis, as well as in methionine synthase.
12 means of controlling cobalamin reactivity in methionine synthase.
13 b5 reconstitute the activity of the porcine methionine synthase.
14 flavodoxin, shuttle electrons from NADPH to methionine synthase.
15 when similar mutations were introduced into methionine synthase.
16 ge for electron transfer to the cobalamin of methionine synthase.
17 ween oxidized flavodoxin and methylcobalamin methionine synthase.
18 inding domain with methylcobalamin-dependent methionine synthase.
19 l portion of the cobalamin-binding region of methionine synthase.
20 ually and in combination in a strain lacking methionine synthase.
21 ity to reduce cytochrome c and to reactivate methionine synthase.
22 le in repairing inactive cobalamin-dependent methionine synthase.
23 h may mediate or facilitate interaction with methionine synthase.
24 in trafficking, and the activation domain of methionine synthase.
25 ontain genes encoding MTHFR and two distinct methionine synthases.
26 ylenetetrahydrofolate reductase (1298AC/CC), methionine synthase (2756AA), and methionine synthase re
28 urally similar to heme and is a cofactor for methionine synthase, a key enzyme in folate metabolism.
29 olymorphisms, which result in less effective methionine synthase activation, do not appear to result
32 iochemical data suggested that low levels of methionine synthase activity in the first patient may re
35 acid into protein, we show that NO inhibits methionine synthase activity in vivo, in cultured mammal
36 tes of cobalamin and that NO's inhibition of methionine synthase activity most likely involves its re
37 ne synthase-deficient patients have residual methionine synthase activity or that humans have a compe
39 cobalamin demand, and management of reduced methionine synthase activity through changes in folate a
40 turbs methionine metabolism by impairment of methionine synthase activity, resulting in deoxynucleosi
43 ino acid starvation test conditions, whereas methionine synthase and acetolactate synthase were not.
44 inactive in vivo in microbial bioassays for methionine synthase and acted as an in vitro inhibitor o
46 try catalyzed by the vitamin B(12)-dependent methionine synthase and is impaired in the cblC group of
47 l by cells of the body that have the enzymes methionine synthase and methyl malonyl CoA mutase, which
48 The recent structures of cobalamin-dependent methionine synthase and methylmalonyl-CoA mutase have re
49 ed for the function of the essential enzymes methionine synthase and methylmalonyl-CoA mutase, respec
53 ional change on binding to the apoenzymes of methionine synthase and methylmalonyl-coenzyme A mutase:
55 nd IDS1; S-adenosyl methionine synthase; and methionine synthase), and other cellular mechanisms (pat
56 dependent enzymes, such as the B12-dependent methionine synthase, and by enzymes involved in the bios
57 bility to serve as a cofactor for the enzyme methionine synthase, and that aquocobalamin could quench
58 rily as a cofactor for vitamin B12-dependent methionine synthase, and that cobalamin auxotrophy has a
59 proteins IDS3a, IDS3b, and IDS1; S-adenosyl methionine synthase; and methionine synthase), and other
62 t for supporting NADPH-dependent activity of methionine synthase at a level that is comparable with t
63 who has an isolated functional deficiency of methionine synthase but appears to be distinct from the
66 ion, they suggest directly that mutations in methionine synthase can lead to elevated homocysteine, i
67 itch from the B. subtilis yitJ gene encoding methionine synthase, can be converted into Spinach ribos
74 These data suggest that genetic variation in methionine synthase could mediate risk of childhood leuk
75 The nitric-oxide-induced inactivation of methionine synthase could offer a rational explanation f
77 born errors resulting in isolated functional methionine synthase deficiency fall into two complementa
80 development in mice and suggest either that methionine synthase-deficient patients have residual met
82 ember of the reductive activation system for methionine synthase describes a function for this protei
83 hat the cblG cell line has defects affecting methionine synthase directly, whereas the cblE cell line
84 s family include the vitamin B(12)-dependent methionine synthases, E. coli S-methylmethionine-S-homoc
85 bamides that were differentially utilized by methionine synthase (EC 2.1.1.13), ethanolamine ammonia-
88 ifts to higher energy when binding to either methionine synthase enzyme, suggesting that there is a s
91 We found little evidence that defects in methionine synthase expression or mutations in the MS ge
96 ructure of the cobalamin-binding fragment of methionine synthase from Escherichia coli (EC 2.1.1.13),
97 ologous to the cobalamin-binding fragment of methionine synthase from Escherichia coli and possessed
100 vide the first evidence for mutations in the methionine synthase gene being culpable for the cblG phe
103 nsic thiol oxidase activity of the mammalian methionine synthase has been proposed to be involved.
105 ase reductase, serves as a redox partner for methionine synthase in an NADPH-dependent reaction.
109 reduced cob(II)alamin for the activation of methionine synthase) indicates a dual physiological role
111 ention of the cobalamin-dependent version of methionine synthase instead of the cobalamin-independent
113 Binding of methylcobalamin to full-length methionine synthase is accompanied by ligand substitutio
114 intermediate, cob(I)alamin, the activity of methionine synthase is additionally dependent on a redox
116 of paramount physiological importance since methionine synthase is an essential enzyme that plays a
119 that the primary role of the ligand triad in methionine synthase is controlling the distribution of e
120 trates, products and downstream metabolites, methionine synthase is directly involved in the sulphur
122 20-fold higher stoichiometry of reductase to methionine synthase is required for NR1 versus methionin
123 ; however, a 3-4-fold higher ratio of MSR to methionine synthase is required to elicit maximal activi
124 nzimidazole on binding of methylcobalamin to methionine synthase, is dissociated from the cobalt of t
126 in CNS function at all ages, especially the methionine-synthase mediated conversion of homocysteine
130 uch that the presence of the B12-independent methionine synthase (METE) enables growth without this v
134 owth because it encodes a B(12) -independent methionine synthase, METE, the gene for which is suppres
150 formin-induced longevity by mutation of worm methionine synthase (metr-1) and S-adenosylmethionine sy
151 that ubiquitously expresses a modified tRNA methionine synthase, metRS, which preferentially incorpo
153 te reductase (MTHFR 677C-->T and 1298A-->C), methionine synthase (MS 2756A-->G), and cystathionine-be
155 ed in intracellular homocysteine management, methionine synthase (MS) and cystathionine beta-synthase
156 anol feeding alone reduced the activities of methionine synthase (MS) and MATIII and increased the ac
161 The folate and vitamin B12-dependent enzyme methionine synthase (MS) is highly sensitive to cellular
162 eine, which can undergo transmethylation via methionine synthase (MS) or transsulfuration via cystath
164 Children with the A2756G polymorphism in methionine synthase (MS) were more likely to demonstrate
165 levels of the homocysteine junction enzymes, methionine synthase (MS), MS reductase (MSR), and cystat
166 20T); reduced folate carrier (RFC G80A); and methionine synthase (MTR A2756G), making the present stu
167 rofolate reductase (MTHFR C677T and A1298C), methionine synthase (MTR A2756G), methionine synthase re
168 teine remethylation/methionine biosynthesis--methionine synthase (MTR) A2756G and methionine synthase
169 hylate homocysteine, vitamin B(12)-dependent methionine synthase (MTR) and betaine-homocysteine methy
170 etrahydrofolate reductase (MTHFR) rs1801133, methionine synthase (MTR) rs1805087 [wild-type (WT)], MT
171 ethylene tetrahydrofolate reductase (MTHFR), methionine synthase (MTR), proton-coupled folate transpo
172 folate reductase [MTHFR] 677C>T and 1298A>C, methionine synthase [MTR] 2756A>G, cystathionine beta-sy
173 e novo dTMP biosynthesis was investigated in methionine synthase-null human fibroblast and nitrous ox
175 tabolic fates: transmethylation catalyzed by methionine synthase or betaine homocysteine methyl trans
176 e two mammalian cobalamin-dependent enzymes, methionine synthase or methylmalonyl-coenzyme A mutase;
177 ormation of a complex between flavodoxin and methionine synthase perturbs the midpoint potentials of
179 12 requirements is defined by the isoform of methionine synthase possessed by an alga, such that the
180 methylation of homocysteine to methionine by methionine synthase), produce more homocysteine thiolact
181 interactions between E. coli flavodoxin and methionine synthase provide a model for the mammalian sy
182 modeled as a reduction in the V(max) of the methionine synthase reaction, results in a secondary fol
186 also showed that purified recombinant human methionine synthase reductase (MSR) in combination with
189 d A1298C), methionine synthase (MTR A2756G), methionine synthase reductase (MTRR A66G), cystathionine
190 te reductase (MTHFR) 677C-->T and 1298A-->C, methionine synthase reductase (MTRR) 66A-->G, and cystat
191 thesis--methionine synthase (MTR) A2756G and methionine synthase reductase (MTRR) A66G--provided evid
194 hylenetetrahydrofolate reductase (MTHFR) and methionine synthase reductase (MTRR), have generated con
196 ytotoxicity was observed in cells expressing methionine synthase reductase (MTRR), novel diflavin oxi
197 tathionine beta-synthase [CBS] 844ins68, and methionine synthase reductase [MTRR] 66A>G) in 452 young
198 cloned and expressed the cDNA encoding human methionine synthase reductase and demonstrate that it is
199 and cblG classes of patients with defects in methionine synthase reductase and methionine synthase, r
200 ptophan in related diflavin reductases (e.g. methionine synthase reductase and novel reductase 1), an
201 of mutations in the gene encoding a putative methionine synthase reductase in the cblE class of patie
202 PH is 2.6 +/- 0.5 microm, and the K(act) for methionine synthase reductase is 80.7 +/- 13.7 nm for NA
206 s, the electron is thought to be provided by methionine synthase reductase, a protein containing a do
207 oxidoreductase with significant homology to methionine synthase reductase, NR1, has been described r
208 he soluble dual flavoprotein oxidoreductase, methionine synthase reductase, serves as a redox partner
209 thionine synthase is required for NR1 versus methionine synthase reductase, suggesting that it may re
216 , the binding of flavodoxin to cob(II)alamin methionine synthase results in a change in the coordinat
217 structure of the cobalamin-binding region of methionine synthase reveals that the cofactor is sandwic
218 CblD, CblC, and the activation domain of methionine synthase share several distinguishing feature
219 ts with an isolated functional deficiency of methionine synthase suggested a role for this protein in
220 holo-MetH protein, a MetH(2-649) fragment of methionine synthase that contains the regions that bind
221 taining both FAD and FMN, and it reactivates methionine synthase that has lost activity due to oxidat
224 e corrin ring; when methylcobalamin binds to methionine synthase, the ligand is replaced by histidine
225 the conversion of the inactive form of human methionine synthase to the active state of the enzyme.
226 r relative affinities for the redox partner, methionine synthase, underlie the differences in the rel
230 residues in the cobalamin-binding region of methionine synthase, we have constructed a synthetic mod
231 ing interface between E. coli flavodoxin and methionine synthase, we have employed site-directed muta
233 e cblG patient has greatly reduced levels of methionine synthase while in another, the enzyme is spec
234 he mutant is depleted in FMN and reactivates methionine synthase with 8% of the efficiency of wild ty
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