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Literature summary for 4.3.99.3 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
Search for more literature for 4.3.99.3

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Burkholderia multivorans A0A0H3KB22
-
-
Burkholderia multivorans ATCC 17616 A0A0H3KB22
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-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CDG synthase
-
 Burkholderia multivorans
queE
-
 Burkholderia multivorans

Cofactor

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