2.1.1.158: 7-methylxanthosine synthase
This is an abbreviated version!
For detailed information about 7-methylxanthosine synthase, go to the full flat file.
Word Map on EC 2.1.1.158
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2.1.1.158
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histone-lysine
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histone
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n-methylation
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methyltransferases
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phosphatidylcholine
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euchromatic
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phosphatidylethanolamine
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methylase
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phenylethanolamine
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s-adenosyl-l-homocysteine
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prmts
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adomet
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zeste
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coffea
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theobromine
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protein-arginine
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s-adenosyl-l-methionine-dependent
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s-adenosylmethionine-dependent
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dimethylaminohydrolase
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phosphatidyl-n-monomethylethanolamine
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guanidinoacetate
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canephora
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ddahs
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agriculture
- 2.1.1.158
-
histone-lysine
- histone
-
n-methylation
- methyltransferases
- phosphatidylcholine
-
euchromatic
- phosphatidylethanolamine
-
methylase
- phenylethanolamine
- s-adenosyl-l-homocysteine
-
prmts
- adomet
-
zeste
- coffea
- theobromine
- protein-arginine
-
s-adenosyl-l-methionine-dependent
-
s-adenosylmethionine-dependent
-
dimethylaminohydrolase
- phosphatidyl-n-monomethylethanolamine
- guanidinoacetate
- canephora
-
ddahs
- agriculture
Reaction
Synonyms
7-methylxanthine 3-N-methyltransferase, 7-methylxanthine synthase, 7-methylxanthosine synthase, 7-methylxanthosine synthase 1, 7-N-methyltransferase, 7NMT, CmXRS1, N-methyltransferase, SAM:xanthosine 7-N-methyltransferase, xanthosine methyltransferase, xanthosine-N7-methyltransferase, xanthosine:S-adenosyl-L-methionine methyltransferase, XMT, XMT1, XRS1
ECTree
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Crystallization
Crystallization on EC 2.1.1.158 - 7-methylxanthosine synthase
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purified recombinant wild-type and selenomethionine-labeled XMT, 23-28% PEG 3350, 0.2 M LiCl, 0.1 M Tris-HCl, pH 8.5-8.7, 2 mM DTT, 1 mM S-adenosyl-L-cysteine, and 1 mM xanthosine, 1-3 days, 20°C, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution
purified recombinant wild-type and selenomethionine-labeled XMT, 23-28% PEG 3350, 0.2 M LiCl, 0.1 M Tris-HCl, pH 8.5-8.7, 2 mM DTT, 2 mM S-adenosyl-L-cysteine, and 2 mM xanthosine, 1-3 days, 20°C, plate-like crystals, X-ray diffraction structure determination and analysis at 2.2 A resolution
using Linbro plates and the conventional hanging-drop technique, in the presence of the demethylated cofactor S-adenosyl-l-cysteine or xanthosine