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1 aine and cob(I)alamin to dimethylglycine and methylcobalamin.
2 pose a methyl group on substrate with one on methylcobalamin.
3  indole nitrogen in Trp during its attack on methylcobalamin.
4  and the methylation of homocysteine by free methylcobalamin.
5 o homocysteine via the enzyme-bound cofactor methylcobalamin.
6  how a protein can control the reactivity of methylcobalamin.
7 stic children were treated with 75 microg/kg methylcobalamin (2 times/wk) and 400 microg folinic acid
8 ine and tetrahydrofolate and is dependent on methylcobalamin, a derivative of vitamin B12, for activi
9                                              Methylcobalamin, a form of vitamin B12 was identified in
10 tic turnover numbers for the dealkylation of methylcobalamin and 5'-deoxyadenosylcobalamin by MMACHC
11 assimilation into the active cofactor forms, methylcobalamin and 5'-deoxyadenosylcobalamin, and is bo
12      The prosthetic group alternates between methylcobalamin and cob(I)alamin during catalysis as hom
13 le, the enzyme alternates between the active methylcobalamin and cob(I)alamin forms of the enzyme.
14 methylated by methyltetrahydrofolate to form methylcobalamin and demethylated by homocysteine to form
15  that targeted nutritional intervention with methylcobalamin and folinic acid may be of clinical bene
16 not treatment with the metabolic precursors, methylcobalamin and folinic acid, would improve plasma c
17 me must alternately stabilize six-coordinate methylcobalamin and four-coordinate cob(I)alamin oxidati
18 rogens in strain DHT3 cell extracts requires methylcobalamin and is inhibited by propyl iodide, a spe
19 min with dimethylsulfide, yielding equimolar methylcobalamin and methanethiol in an endergonic reacti
20 ponsible for binding of the prosthetic group methylcobalamin, and amino acids 897-1227 are involved i
21 e examined the binding of adenosylcobalamin, methylcobalamin, and cob(II)alamin to the enzyme.
22 ions included vitamin B12, the B12 coenzyme, methylcobalamin, and dicyanocobyrinic acid heptamethyles
23 , in a reaction that is first-order in added methylcobalamin, and we have confirmed this observation
24 olism, the organocobalamins coenzyme B12 and methylcobalamin, are highly photolabile, as are other al
25 talyze methylation of homocysteine with free methylcobalamin as the methyl donor, in a reaction that
26                  Notably, TaCblC dealkylates methylcobalamin at a rate ca. 2-times higher than HsCblC
27 leotide substituent of the corrin ring; when methylcobalamin binds to methionine synthase, the ligand
28 by dimethylsulfide was mixed with respect to methylcobalamin, but competitive with coenzyme M.
29 ond-order rate constant for demethylation of methylcobalamin by Hcy is elevated 60-fold and that for
30 n polyacrylamide gels revealed an additional methylcobalamin:coenzyme M (methylcobalamin:CoM) methylt
31 ferase composed of two polypeptides, MtsA (a methylcobalamin:coenzyme M methyltransferase) and MtsB (
32                            MtsA is an active methylcobalamin:coenzyme M methyltransferase, but also m
33                    Dimethylsulfide inhibited methylcobalamin:coenzyme methyl transfer by MtsA.
34 folate to the cob(I)alamin cofactor, forming methylcobalamin cofactor and tetrahydrofolate prior to t
35 In the E. coli enzyme, the lower face of the methylcobalamin cofactor is coordinated by histidine 759
36 -285 in methyl coenzyme M reductase, binds a methylcobalamin cofactor required for methyl transfer fr
37 the enzyme transfers a methyl group from the methylcobalamin cofactor to homocysteine, generating cob
38 ormational change accompanies binding of the methylcobalamin cofactor.
39 or serine 810 decrease the reactivity of the methylcobalamin cofactor.
40  to the N termini of the A and M isozymes of methylcobalamin:CoM methyltransferase (methyltransferase
41                                          The methylcobalamin:CoM methyltransferase activity of the pu
42 ent molecular mass of 48 kDa which possessed methylcobalamin:CoM methyltransferase activity was detec
43 ed an additional methylcobalamin:coenzyme M (methylcobalamin:CoM) methyltransferase present in cells
44 f cob(I)alamin during turnover, to an active methylcobalamin-containing form requires a reductive met
45 cofactor for adenosylcobalamin-dependent and methylcobalamin-dependent enzymes, it plays a crucial ro
46 urally similar cobalamin-binding domain with methylcobalamin-dependent methionine synthase.
47  adenosylcobalamin-dependent isomerases, the methylcobalamin-dependent methyltransferases, and the de
48 cobalamin was completely decyanated to [13C]-methylcobalamin describing metabolic utilization, and it
49 oA was formed in reactions with CoA, CO, and methylcobalamin, directly demonstrating C-C bond activat
50                             Demethylation of methylcobalamin enzyme also leads to cob(I)alamin format
51 in can also be generated by demethylation of methylcobalamin enzyme by homocysteine; it was not known
52  initially in formation of a five-coordinate methylcobalamin enzyme that slowly decays to the active
53 atalyzes the transfer of a methyl group from methylcobalamin enzyme to homocysteine, generating methi
54 rahydrofolate is already present on the free methylcobalamin enzyme.
55 t slowly decays to the active six-coordinate methylcobalamin enzyme.
56 rating tetrahydrofolate and regenerating the methylcobalamin enzyme.
57  L-methylfolate, pyridoxal 5'-phosphate, and methylcobalamin for management of endothelial dysfunctio
58                   The results imply that the methylcobalamin form of MetH exists as an ensemble of in
59 e cobalt, restoring the enzyme to the active methylcobalamin form.
60 cobalamin, cyanocobalamin, hydroxocobalamin, methylcobalamin) from dietary ingredients and supplement
61           The Cys310Ala and Cys311Ala mutant methylcobalamin holoenzymes have completely lost the abi
62 It has four bioactive forms: cyanocobalamin, methylcobalamin, hydroxocobalamin and 5'-deoxyadenosylco
63 The lower axial ligand to the cobalt in free methylcobalamin is the dimethylbenzimidazole nucleotide
64 hydrofolate to homocysteine via the cofactor methylcobalamin, is one of the two established mammalian
65  electrochemical (EC) reduction mechanism of methylcobalamin (Me-Cbl) in a mixed DMF/MeOH solvent in
66  reaction monitoring (MRM) and identified as methylcobalamin (Me-Cbl).
67                          The B(12) cofactors methylcobalamin (MeCbl) and 5'-deoxyadenosylcobalamin (A
68 l activity of adenosylcobalamin (AdoCbl) and methylcobalamin (MeCbl) is the Co-C bond cleavage step.
69 he native cofactor AdoCbl and its derivative methylcobalamin (MeCbl).
70  [H2O-Cbl], adenosylcobalamin [Ado-Cbl], and methylcobalamin [MeCbl]), only the H2O-Cbl combined with
71 nd the dealkylation of alkylcobalamins (e.g. methylcobalamin; MeCbl).
72 ing was seen between oxidized flavodoxin and methylcobalamin methionine synthase.
73  treat patients, including hydroxocobalamin, methylcobalamin, methionine and betaine.
74  by heterolytic cleavage of the Co-C bond in methylcobalamin or the two-electron reduction of vitamin
75 y oxidation of cob(I)alamin or photolysis of methylcobalamin renders the enzyme inactive.
76 ation as the newly remethylated 5-coordinate methylcobalamin returns to the 6-coordinate state, trigg
77 ylmethionine returns the enzyme to an active methylcobalamin state.
78 djacently encoded protein, was shown to be a methylcobalamin:tetrahydrofolate methyltransferase and i
79                                   Binding of methylcobalamin to full-length methionine synthase is ac
80 etely abolish methyl transfer from exogenous methylcobalamin to homocysteine but do not affect methyl
81  protein catalyzes methyl transfer from free methylcobalamin to homocysteine but not from methyltetra
82 he ability to transfer the methyl group from methylcobalamin to homocysteine, suggesting that zinc is
83 es the transfer of a methyl group from bound methylcobalamin to homocysteine, yielding enzyme-bound c
84 ity to transfer methyl groups from exogenous methylcobalamin to homocysteine.
85 r ligand dimethylbenzimidazole on binding of methylcobalamin to methionine synthase, is dissociated f
86  cycle, the cobalamin-binding domain carries methylcobalamin to the homocysteine (Hcy) domain to form
87                              Weak binding to methylcobalamin was indicated by the apparent Km of 14 m
88 ention trial with folinic acid, betaine, and methylcobalamin was initiated in a subset of the autisti
89 d NADPH, holoenzyme formation from apoMS and methylcobalamin was significantly enhanced.
90 e to metabolize cobalamin into adenosyl- and methylcobalamin, which results in the biochemical pertur
91  methylcobinamide reacts 35-fold faster than methylcobalamin with enzyme-bound tetrahydrofolate.