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ChemBioChem, ISSN 1439-4227, 01/2015, Volume 16, Issue 1, pp. 119 - 125
Ergothioneine is an N‐α‐trimethyl‐2‐thiohistidine derivative that occurs in human, plant, fungal, and bacterial cells. Biosynthesis of this redox‐active... 
betaines | ergothioneine | methyltransferases | hypaphorine | amino acids | biosynthesis | Amino acids | Biosynthesis ergothioneine | Methyltransferases | Hypaphorine | Betaines | CHEMISTRY, MEDICINAL | TRANSPORTER | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTALLOGRAPHY | PROTECTS | ANTIOXIDANT | REDESIGN | TOOL | Fungal Proteins - chemistry | S-Adenosylhomocysteine - metabolism | Betaine - metabolism | Methyltransferases - metabolism | Methyltransferases - genetics | Molecular Sequence Data | Substrate Specificity | Tryptophan - chemistry | Crystallography, X-Ray | S-Adenosylmethionine - chemistry | Ergothioneine - metabolism | Histidine - metabolism | Tryptophan - metabolism | Ergothioneine - chemistry | Basidiomycota - enzymology | Ascomycota - genetics | Escherichia coli - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Methyltransferases - chemistry | Catalytic Domain | Gene Expression | S-Adenosylhomocysteine - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Ascomycota - enzymology | Recombinant Proteins - genetics | Fungal Proteins - genetics | Sequence Homology, Amino Acid | Betaine - chemistry | Sequence Alignment | Escherichia coli - genetics | Basidiomycota - genetics | Mutation | Histidine - chemistry | S-Adenosylmethionine - metabolism | Fungal Proteins - metabolism | Transferases | Genomics | Crystals | Physiological aspects | Tryptophan | Biosynthesis | Structure | Bacteriology | Substrates
Journal Article
Journal Article
Acta Crystallographica Section D, ISSN 1399-0047, 12/2015, Volume 71, Issue 12, pp. 2422 - 2432
S‐Adenosyl‐L‐homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S‐adenosyl‐L‐methionine (SAM)‐dependent methylation reactions. After... 
adenosine | homocysteine | nicotinamide adenine dinucleotide | S‐adenosyl‐L‐homocysteine | S‐adenosyl‐L‐homocysteine hydrolase | S‐adenosyl‐L‐methionine | nitrogen fixation | plant–bacteria interactions | S-adenosyl-l-homocysteine | Adenosine | S-adenosyl-l-homocysteine hydrolase | Nicotinamide adenine dinucleotide | Nitrogen fixation | S-adenosyl-l-methionine | Homocysteine | Plant-bacteria interactions | RAT-LIVER | CRYSTALLIZATION | plant-bacteria interactions | MECHANISM | 2-DEOXYADENOSINE | S-adenosyl-L-homocysteine hydrolase | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | S-adenosyl-L-homocysteine | CRYSTALLOGRAPHY | BINDING PROTEIN | SITE-DIRECTED MUTAGENESIS | INACTIVATION | BIOPHYSICS | ADENOSYLHOMOCYSTEINE HYDROLASE | SUBSTRATE | PURIFICATION | S-adenosyl-L-methionine | S-Adenosylhomocysteine - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Crystallography, X-Ray | Homocysteine - metabolism | S-Adenosylmethionine - chemistry | Protein Subunits - metabolism | NAD - chemistry | Adenosylhomocysteinase - genetics | Escherichia coli - metabolism | Adenosine - chemistry | Binding Sites | NAD - metabolism | Protein Subunits - genetics | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Gene Expression | Biocatalysis | S-Adenosylhomocysteine - chemistry | Protein Structure, Secondary | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Adenosylhomocysteinase - metabolism | Bradyrhizobium - chemistry | Recombinant Proteins - genetics | Adenosylhomocysteinase - chemistry | Bradyrhizobium - enzymology | Escherichia coli - genetics | Adenosine - metabolism | Protein Binding | Bacterial Proteins - metabolism | Protein Subunits - chemistry | Homocysteine - chemistry | S-Adenosylmethionine - metabolism | Niacinamide | Purines | Enzymes | Crystals | Hydrolases | Structure | Methylation
Journal Article
Current Topics in Medicinal Chemistry, ISSN 1568-0266, 11/2016, Volume 16, Issue 28, pp. 3258 - 3273
Journal Article
Molecular Cell, ISSN 1097-2765, 2003, Volume 12, Issue 1, pp. 177 - 185
DIM-5 is a SUV39-type histone H3 Lys9 methyltransferase that is essential for DNA methylation in N. crassa. We report the structure of a ternary complex... 
SITE | DNA METHYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SET DOMAIN PROTEINS | CATALYTIC MECHANISM | ACTIVE GENES | NEUROSPORA-CRASSA | CELL BIOLOGY
Journal Article
Journal Article
Journal Article
Nature Structural and Molecular Biology, ISSN 1545-9993, 03/2009, Volume 16, Issue 3, pp. 312 - 317
Journal Article
Nucleic Acids Research, ISSN 0305-1048, 09/2017, Volume 45, Issue 15, pp. 9019 - 9029
Journal Article