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Literature summary extracted from

  • Jaeger, C.M.; Croft, A.K.
    Radical reaction control in the AdoMet radical enzyme CDG synthase (QueE) consolidate, destabilize, accelerate (2017), Chemistry, 23, 953-962 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.99.3 Mg2+ the Mg2+ complexation not only brings the substrate into the reactive conformation but also, once a hydrogen atom is abstracted from the substrate, holds the resultant intermediate radical in a highly strained conformation Burkholderia multivorans

Organism

EC Number Organism UniProt Comment Textmining
4.3.99.3 Burkholderia multivorans A0A0H3KB22
-
-
4.3.99.3 Burkholderia multivorans ATCC 17616 A0A0H3KB22
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.99.3 6-carboxy-5,6,7,8-tetrahydropterin
-
Burkholderia multivorans 7-carboxy-7-carbaguanine + NH3
-
?
4.3.99.3 6-carboxy-5,6,7,8-tetrahydropterin
-
Burkholderia multivorans ATCC 17616 7-carboxy-7-carbaguanine + NH3
-
?

Synonyms

EC Number Synonyms Comment Organism
4.3.99.3 CDG synthase
-
Burkholderia multivorans
4.3.99.3 queE
-
Burkholderia multivorans

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.99.3 S-adenosyl-L-methionine S-adenosyl-L-methionine-dependent radical enzyme Burkholderia multivorans