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5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity

Known as: homocysteine methylase activity, MetE, methionine synthase (cobalamin-independent) activity 
Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate. [EC:2.1.1.14… 
National Institutes of Health

Papers overview

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Review
2015
Review
2015
Low molecular weight (LMW) thiols function as thiol-redox buffers to maintain the reduced state of the cytoplasm. The best… 
Highly Cited
2011
Highly Cited
2011
Protein S-thiolation is a post-translational thiol-modification that controls redox-sensing transcription factors and protects… 
Highly Cited
2004
Highly Cited
2004
Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L… 
Highly Cited
2001
Highly Cited
2001
X-ray absorption spectroscopy has been used to investigate binding of selenohomocysteine to cobalamin-independent (MetE) and… 
Highly Cited
1999
Highly Cited
1999
Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from… 
Review
1998
Review
1998
at least two types of block may be involved: a fast electriRecent recognition of sperm limitation effects, and quancal block… 
Highly Cited
1996
Highly Cited
1996
Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from… 
Highly Cited
1995
Highly Cited
1995
Methionine synthases catalyze the formation of methionine by the transfer of a methyl group from 5-methyltetrahydrofolate to… 
Highly Cited
1987
Highly Cited
1987
We isolated an Escherichia coli methionine auxotroph that displays a growth phenotype similar to that of known metF mutants but…