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Literature summary for 2.1.1.349 extracted from

  • Fenwick, M.; Philmus, B.; Begley, T.; Ealick, S.
    Burkholderia glumae ToxA is a dual-specificity methyltransferase that catalyzes the last two steps of toxoflavin biosynthesis (2016), Biochemistry, 55, 2748-2759 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.349

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Burkholderia glumae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Burkholderia glumae

Protein Variants

Protein Variants Comment Organism
Y7A structures of the mutant enzyme show an open active site, suggesting that the hydroxyl group of Tyr7 plays a role in opening and closing the active site during the multistep reaction Burkholderia glumae
Y7F crystal structures of mutant enzyme consistently show a closed active site Burkholderia glumae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin Burkholderia glumae the enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens S-adenosyl-L-homocysteine + reumycin
-
 ?
S-adenosyl-L-methionine + reumycin Burkholderia glumae the enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens S-adenosyl-L-homocysteine + toxoflavin
-
 ?

Organism

Organism UniProt Comment Textmining
Burkholderia glumae Q9LBJ0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Burkholderia glumae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin
-
 Burkholderia glumae S-adenosyl-L-homocysteine + reumycin
-
 ?
S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin the enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens Burkholderia glumae S-adenosyl-L-homocysteine + reumycin
-
 ?
S-adenosyl-L-methionine + reumycin
-
 Burkholderia glumae S-adenosyl-L-homocysteine + toxoflavin
-
 ?
S-adenosyl-L-methionine + reumycin the enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens Burkholderia glumae S-adenosyl-L-homocysteine + toxoflavin
-
 ?

Synonyms

Synonyms Comment Organism
toxA
-
 Burkholderia glumae

General Information

General Information Comment Organism
malfunction toxA knockouts of Burkholderia glumae are less virulent in plant infection models Burkholderia glumae
metabolism the enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens Burkholderia glumae