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Literature summary extracted from

  • McCarty, R.M.; Krebs, C.; Bandarian, V.
    Spectroscopic, steady-state kinetic, and mechanistic characterization of the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines (2013), Biochemistry, 52, 188-198.
    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) Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.99.3 additional information
-
 additional information steady-state kinetics, overview Bacillus subtilis
4.3.99.3 0.02
-
 6-carboxy-5,6,7,8-tetrahydropterin pH 7,4, temperature not specified in the publication, recombinant enzyme Bacillus subtilis

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 Bacillus subtilis
4.3.99.3 Mg2+ dependent on, Km is 0.21 mM Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.99.3 29000
-
 2 * 29000, recombinant enzyme, SDS-PAGE Bacillus subtilis

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 Bacillus subtilis
-
 7-carboxy-7-carbaguanine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.99.3 Bacillus subtilis
-
-
-

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 Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.3.99.3 6-carboxy-5,6,7,8-tetrahydropterin = 7-carboxy-7-carbaguanine + NH3 reaction mechanism Bacillus subtilis
a

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
-
 Bacillus subtilis 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 Bacillus subtilis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.99.3 dimer 2 * 29000, recombinant enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
4.3.99.3 CDG synthase
-
 Bacillus subtilis
4.3.99.3 queE
-
 Bacillus subtilis
4.3.99.3 ToyC
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.99.3 5.4
-
 6-carboxy-5,6,7,8-tetrahydropterin pH 7,4, temperature not specified in the publication, recombinant enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.99.3 7.4
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.99.3 S-adenosyl-L-methionine Km is 0.045 mM, the cofactor supports multiple turnovers, it is regenerated at the end of each catalytic cycle Bacillus subtilis

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, all of which use 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 Bacillus subtilis
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 Bacillus subtilis
4.3.99.3 additional information mechanism of rearrangement of the enzyme Bacillus subtilis