EC Number   |
General Information |
Reference |
|---|
    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 |
729229 |
| 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 |
730439 |
| 4.3.99.3 | evolution |
QueE is a member of the radical SAM organic radical generating enzyme superfamily. Members of the radical SAM superfamily contain a CX3CX2C-motif for binding a [4Fe-4S] cluster, which when reductively activated, cleaves SAM to 5'-deoxyadenosyl radical, which in turn initiates radical mediated transformations of the substrate |
717240 |
| 4.3.99.3 | metabolism |
QueE is involved in the queuosine biosynthetic pathway of Bacillus subtilis |
717240 |
| 4.3.99.3 | metabolism |
the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products |
-, 748040 |
| 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 |
729229, 730439 |
| 4.3.99.3 | more |
mechanism of rearrangement of the enzyme |
729229 |
| 4.3.99.3 | more |
substrate binding generates a metal-binding site |
730439 |
