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IUBMB CommentsThe enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
homocysteine methyltransferase, homocysteine s-methyltransferase, athmt-1, homocysteine transmethylase, l-homocysteine s-methyltransferase, yagd protein, s-methylmethionine homocysteine methyltransferase, athmt-2,
more
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adenosylmethionine transmethylase
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adenosylmethionine:homocysteine methyltransferase
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homocysteine methylase
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homocysteine methyltransferase
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homocysteine transmethylase
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L-homocysteine S-methyltransferase
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methylmethionine:homocysteine methyltransferase
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S-adenosyl-L-methionine:L-homocysteine methyltransferase
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S-adenosylmethionine homocysteine transmethylase
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S-adenosylmethionine-homocysteine transmethylase
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S-adenosylmethionine:homocysteine methyltransferase
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S-methylmethionine homocysteine transmethylase
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AtHMT-1
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AtHMT-1
encoded by single copy gene
AtHMT-2
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AtHMT-2
encoded by single copy gene
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methyl group transfer
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S-adenosyl-L-methionine:L-homocysteine S-methyltransferase
The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine.
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
S-methyl-L-methionine + L-cysteine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
S-methyl-L-methionine + L-homocysteine
2 L-methionine
additional information
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the Km-value for S-adenosyl-L-methionine is higher than for S-methyl-L-methionine and the Vmax value is lower
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the Km-value for S-adenosyl-L-methionine is higher than for S-methyl-L-methionine and the Vmax value is lower
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the Km-value for S-adenosyl-L-methionine is higher than for S-methyl-L-methionine and the Vmax value is lower
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
synthesis of L-methionine from homocysteine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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additional information
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no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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additional information
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no activity with DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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additional information
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no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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additional information
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no activity with D-cysteine, L-cysteine, DL-selenocysteine, glutathione, coenzyme A, sulfide, or thiocyanate
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-adenosyl-L-methionine + L-homocysteine
S-adenosyl-L-homocysteine + L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
S-methyl-L-methionine + L-homocysteine
2 L-methionine
synthesis of L-methionine from homocysteine
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S-methyl-L-methionine + L-homocysteine
2 L-methionine
the enzyme uses S-methyl-L-methionine and S-adenosyl-L-methionine as methyl donor in vivo
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additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
additional information
contains a zinc-binding motif, no stimulation by 0.1 or 1 mM Zn2+
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EDTA
1 mM, 26% inhibition
L-methionine
strong product inhibition
additional information
no product inhibition by L-methionine below 0.5 mM, no inhibition by EDTA
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additional information
no product inhibition by L-methionine below 0.5 mM, no inhibition by EDTA
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0.067 - 0.077
L-homocysteine
1.95
S-adenosyl-L-methionine
pH 7.5, 30°C
0.029
S-methyl-L-methionine
pH 7.5, 30°C
0.018 - 0.035
L-homocysteine
0.225 - 1.76
S-adenosyl-L-methionine
0.05 - 0.335
S-methyl-L-methionine
0.067
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine
0.077
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine
0.018
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine
0.027
L-homocysteine
pH 7.5, 25°C, cosubstrate: S-adenosyl-L-methionine
0.03
L-homocysteine
pH 7.5, 25°C, cosubstrate: S-methyl-L-methionine
0.035
L-homocysteine
pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine
0.225
S-adenosyl-L-methionine
pH 7.5, 30°C
1.76
S-adenosyl-L-methionine
pH 7.5, 25°C
0.05
S-methyl-L-methionine
pH 7.5, 30°C
0.335
S-methyl-L-methionine
pH 7.5, 25°C
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SwissProt
brenda
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rosette leaves, cauline leaves
brenda
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brenda
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brenda
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brenda
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brenda
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HMT1_ARATH
326
0
35980
Swiss-Prot
other Location (Reliability: 3)
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36400
1 * 36400, calculated from sequence
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monomer
1 * 36000, calculated from sequence
monomer
1 * 36400, calculated from sequence
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expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
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Ranocha, P.; Bourgis, F.; Ziemak, M.J.; Rhodes, D.; Gage, D.A.; Hanson, A.D.
Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis
J. Biol. Chem.
275
15962-15968
2000
Arabidopsis thaliana (Q9M1W4), Arabidopsis thaliana (Q9SDL7)
brenda
Ranocha, P.; McNeil, S.D.; Ziemak, M.J.; Li, C.; Tarczynski, M.C.; Hanson, A.D.
The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity
Plant J.
25
575-584
2001
Arabidopsis thaliana (Q8LAX0)
brenda