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Literature summary extracted from

  • Dowling, D.P.; Bruender, N.A.; Young, A.P.; McCarty, R.M.; Bandarian, V.; Drennan, C.L.
    Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism (2014), Nat. Chem. Biol., 10, 106-112.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.99.3 recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Burkholderia multivorans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.99.3 purified His6-tagged enzyme in complex with substrate 6-carboxy-5,6,7,8-tetrahydropterin and cofactor S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2-2.6 A resolution Burkholderia multivorans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.3.99.3 Fe2+ the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine, a single [4Fe-4S] cluster per monomer. The cluster-binding motifs of each monomer are located at opposite ends of the dimer molecule, of the Fe atoms from the cluster are coordinated by three cysteine residues from the CX14CXPhiC motif. The remaining unique Fe binds the alpha-amino and alpha-carboxyl groups of S-adenosyl-L-methionine, which adopts an anti orientation about the glycosidic bond Burkholderia multivorans
4.3.99.3 Mg2+ dependent on, the ligand environment about Mg2+ is pseudo-octahedral, with three water ligands, the substrate C4 carbonyl and C6 carboxylate oxygens, and the hydroxyl of T51 Burkholderia multivorans

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.99.3 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Burkholderia multivorans

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 the substrate binds perpendicular to the [4Fe-4S]-bound S-adenosyl-L-methionine cofactor, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg2+, which directly coordinates to the substrate. Substrate binding generates a metal-binding site Burkholderia multivorans 7-carboxy-7-carbaguanine + NH3
-
 ?
4.3.99.3 additional information the enzyme uses a bound [4Fe-4S]+ cluster to catalyze the reductive cleavage of S-adenosyl-L-methionine cofactor to generate methionine and a 5'-deoxyadenosyl radical, which initiates enzymatic transformations requiring H-atom abstraction. To initiate radical chemistry, all AdoMet radical enzymes require the one-electron reduction of the [4Fe-4S] cluster. This electron is typically supplied by a flavodoxin. For the Burkholderia multivorans enzyme, more product is generated using the chemical reductant dithionite Burkholderia multivorans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.99.3 dimer
-
 Burkholderia multivorans

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.99.3 7.4
-
 assay at Burkholderia multivorans

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.99.3 additional information to initiate radical chemistry, all AdoMet radical enzymes require the one-electron reduction of the [4Fe-4S] cluster. This electron is typically supplied by a flavodoxin. For the Burkholderia multivorans enzyme, more product is generated using the chemical reductant dithionite Burkholderia multivorans
4.3.99.3 S-adenosyl-L-methionine the binding site is conserved despite modified enzyme fold Burkholderia multivorans

General Information

EC Number General Information Comment Organism
4.3.99.3 evolution QueE is a member of the radical S-adenosyl-L-methionine superfamily, it varies from the other members in that it contains a hypermodified (beta6/alpha3) protein core and an expanded cluster-binding motif CX14CX2C, structure comparisons, overview Burkholderia multivorans
4.3.99.3 metabolism the enzyme catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin to 7-carboxy-7-carbaguanine in the third step of the biosynthetic pathway to all 7-deazapurines. 7-Carboxy-7-carbaguanine is the first 7-deazapurine in the biosynthetic pathway and likely the precursor to all naturally occurring 7-deazapurine containing molecules Burkholderia multivorans
4.3.99.3 additional information substrate binding generates a metal-binding site Burkholderia multivorans