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Literature summary for 4.3.99.3 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics, overview | Bacillus subtilis | |
| 0.02 | - |
6-carboxy-5,6,7,8-tetrahydropterin | pH 7,4, temperature not specified in the publication, recombinant enzyme | Bacillus subtilis |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| Mg2+ | dependent on, Km is 0.21 mM | Bacillus subtilis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 29000 | - |
2 * 29000, recombinant enzyme, SDS-PAGE | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 6-carboxy-5,6,7,8-tetrahydropterin | Bacillus subtilis | - |
7-carboxy-7-carbaguanine + NH3 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Bacillus subtilis |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 6-carboxy-5,6,7,8-tetrahydropterin = 7-carboxy-7-carbaguanine + NH3 | reaction mechanism | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 6-carboxy-5,6,7,8-tetrahydropterin | - |
Bacillus subtilis | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 29000, recombinant enzyme, SDS-PAGE | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CDG synthase | - |
Bacillus subtilis |
| queE | - |
Bacillus subtilis |
| ToyC | - |
Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 5.4 | - |
6-carboxy-5,6,7,8-tetrahydropterin | pH 7,4, temperature not specified in the publication, recombinant enzyme | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| additional information | mechanism of rearrangement of the enzyme | Bacillus subtilis |
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