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5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
Known as:
homocysteine methylase activity
, MetE
, methionine synthase (cobalamin-independent) activity
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Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate. [EC:2.1.1.14…
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National Institutes of Health
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2015
Review
2015
Redox regulation by reversible protein S-thiolation in bacteria
V. V. Loi
,
Martina Rossius
,
H. Antelmann
Frontiers in Microbiology
2015
Corpus ID: 16772046
Low molecular weight (LMW) thiols function as thiol-redox buffers to maintain the reduced state of the cytoplasm. The best…
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Highly Cited
2011
Highly Cited
2011
S-Bacillithiolation Protects Against Hypochlorite Stress in Bacillus subtilis as Revealed by Transcriptomics and Redox Proteomics*
B. Chi
,
Katrin Gronau
,
U. Mäder
,
Bernd Hessling
,
D. Becher
,
H. Antelmann
Molecular & Cellular Proteomics
2011
Corpus ID: 7545409
Protein S-thiolation is a post-translational thiol-modification that controls redox-sensing transcription factors and protects…
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Highly Cited
2004
Highly Cited
2004
Cobalamin-Independent Methionine Synthase (MetE): A Face-to-Face Double Barrel That Evolved by Gene Duplication
R. Pejchal
,
M. Ludwig
PLoS Biology
2004
Corpus ID: 8185244
Cobalamin-independent methionine synthase (MetE) catalyzes the transfer of a methyl group from methyltetrahydrofolate to L…
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Highly Cited
2003
Highly Cited
2003
Genome-wide analysis of the L-methionine biosynthetic pathway in Corynebacterium glutamicum by targeted gene deletion and homologous complementation.
C. Rückert
,
A. Pühler
,
Jörn Kalinowski
Journal of Biotechnology
2003
Corpus ID: 22889180
Highly Cited
2001
Highly Cited
2001
Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy.
K. Peariso
,
Zhaohui Sunny Zhou
,
April E. Smith
,
R. Matthews
,
J. Penner‐Hahn
Biochemistry
2001
Corpus ID: 6919345
X-ray absorption spectroscopy has been used to investigate binding of selenohomocysteine to cobalamin-independent (MetE) and…
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Highly Cited
1999
Highly Cited
1999
Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli.
Z. Zhou
,
K. Peariso
,
J. Penner‐Hahn
,
R. Matthews
Biochemistry
1999
Corpus ID: 46091352
Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from…
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Review
1998
Review
1998
Polyspermy, Egg Size, and the Fertilization Kinetics of Free‐Spawning Marine Invertebrates
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…
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Highly Cited
1996
Highly Cited
1996
Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme.
Julio C. González
,
K. Peariso
,
J. Penner‐Hahn
,
R. Matthews
Biochemistry
1996
Corpus ID: 23733550
Cobalamin-independent methionine synthase (MetE) from Escherichia coli catalyzes the transfer of a methyl group from…
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Highly Cited
1995
Highly Cited
1995
Vitamin-B12-independent methionine synthase from a higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties.
J. Eichel
,
Julio C. González
,
M. Hotze
,
R. Matthews
,
J. Schröder
European Journal of Biochemistry
1995
Corpus ID: 12903223
Methionine synthases catalyze the formation of methionine by the transfer of a methyl group from 5-methyltetrahydrofolate to…
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Highly Cited
1987
Highly Cited
1987
A new methionine locus, metR, that encodes a trans-acting protein required for activation of metE and metH in Escherichia coli and Salmonella typhimurium
M. Urbanowski
,
L. T. Stauffer
,
L. Plamann
,
G. Stauffer
Journal of Bacteriology
1987
Corpus ID: 46382320
We isolated an Escherichia coli methionine auxotroph that displays a growth phenotype similar to that of known metF mutants but…
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