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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
2013
Highly Cited
2013
AIMS Protein S-bacillithiolations are mixed disulfides between protein thiols and the bacillithiol (BSH) redox buffer that occur… 
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
2005
Highly Cited
2005
  • F. Studier
  • Protein Expression and Purification
  • 2005
  • Corpus ID: 7708414
Highly Cited
2005
Highly Cited
2005
Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L… 
Highly Cited
2004
Highly Cited
2004
In nature, Escherichia coli are exposed to harsh and non-ideal growth environments—nutrients may be limiting, and cells are often… 
Review
1998
Review
1998
  • C. Styan
  • American Naturalist
  • 1998
  • Corpus ID: 20722853
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
1992
Highly Cited
1992
In Escherichia coli, two enzymes catalyze the synthesis of methionine from homocysteine using methyltetrahydrofolate as the donor…