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Gene Review:

ECs4759 - 5-methyltetrahydropteroyltriglutamate/homo...

Escherichia coli O157:H7 str. Sakai

Hondorp, E.R. et al., Pejchal, R. et al., Leichert, L.I. et al., Vaupel, M. et al., González, J.C. et al., et al.

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Disease relevance of ECs4759

Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme [1].

High impact information on ECs4759

Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine to form tetrahydrofolate and methionine [2].
Protonolysis of [Ph(pztBu)-BttBu]Zn(CH3) by PhSH in toluene yielded [Ph(pztBu)BttBu]Zn(SPh), a synthetic analogue of the homocysteine ligated form of cobalamin-independent methionine synthase (Met E) [3].
Upstream of the mch gene two open reading frames were recognized, one encoding for a 25-kDa protein with sequence similarity to deoxyuridylate hydroxymethylase and the other encoding for a 34.6-kDa protein with sequence similarity to cobalamin-independent methionine synthase (MetE) [4].
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication [5].
Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli [6].

Chemical compound and disease context of ECs4759

Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine [1].
For E. coli cells confronting these realities, there appears to be a link between oxidative stress, methionine availability, and the enzyme that catalyzes the final step of methionine biosynthesis, cobalamin-independent methionine synthase (MetE) [6].

Associations of ECs4759 with chemical compounds

Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L-homocysteine (Hcy) without using an intermediate methyl carrier [5].
H(2)O(2)-induced oxidative stress resulted in the specific oxidation of thiols of proteins involved in detoxification of H(2)O(2) and of enzymes of cofactor and amino acid biosynthesis pathways such as thiolperoxidase, GTP-cyclohydrolase I, and the cobalamin-independent methionine synthase MetE [7].

References

Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme. González, J.C., Peariso, K., Penner-Hahn, J.E., Matthews, R.G. Biochemistry (1996) [Pubmed]
Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Zhou, Z.S., Peariso, K., Penner-Hahn, J.E., Matthews, R.G. Biochemistry (1999) [Pubmed]
Synthetic models for the zinc sites in the methionine synthases. Chiou, S.J., Innocent, J., Riordan, C.G., Lam, K.C., Liable-Sands, L., Rheingold, A.L. Inorganic chemistry. (2000) [Pubmed]
Primary structure of cyclohydrolase (Mch) from Methanobacterium thermoautotrophicum (strain Marburg) and functional expression of the mch gene in Escherichia coli. Vaupel, M., Dietz, H., Linder, D., Thauer, R.K. Eur. J. Biochem. (1996) [Pubmed]
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication. Pejchal, R., Ludwig, M.L. PLoS Biol. (2005) [Pubmed]
Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli. Hondorp, E.R., Matthews, R.G. PLoS Biol. (2004) [Pubmed]
Protein thiol modifications visualized in vivo. Leichert, L.I., Jakob, U. PLoS Biol. (2004) [Pubmed]

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