Crystallization (Comment) | Organism |
---|---|
X-ray crystal structure of dimeric His6 tagged enzyme is determined to 2.55 A resolution by Multiwavelength Anomalous Dispersion | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | Mg2+ provides key contacts with the substrate 6-carboxy-5,6,7,8-tetrahydropterin and the product 7-carboxy-7-carbaguanine, thus anchoring the molecules in the active site. The formation of either 6-carboxypterin product is not enhanced by the presence of Mg2+ | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-carboxy-5,6,7,8-tetrahydropterin | Bacillus subtilis | the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
6-carboxy-5,6,7,8-tetrahydropterin | Bacillus subtilis 168 | the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products | 7-carboxy-7-carbaguanine + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O31677 | - |
- |
Bacillus subtilis 168 | O31677 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
6-carboxy-5,6,7,8-tetrahydropterin | - |
Bacillus subtilis | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
6-carboxy-5,6,7,8-tetrahydropterin | the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products | Bacillus subtilis | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
6-carboxy-5,6,7,8-tetrahydropterin | - |
Bacillus subtilis 168 | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
6-carboxy-5,6,7,8-tetrahydropterin | the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products | Bacillus subtilis 168 | 7-carboxy-7-carbaguanine + NH3 | - |
? | |
6-carboxypterin | under reducing conditions that would promote the reductive cleavage of S-adenosyl-L-methionine, 6-carboxypterin is turned over to 6-deoxyadenosylpterin, presumably by radical addition of the 5'-deoxyadenosine followed by oxidative decarboxylation to the product. In the absence of the strong reductant, dithionite, the carboxylate of 6-carboxypterin is esterified to generate 6-carboxypterin-5'-deoxyadenosyl ester | Bacillus subtilis | ? | - |
? | |
6-carboxypterin | under reducing conditions that would promote the reductive cleavage of S-adenosyl-L-methionine, 6-carboxypterin is turned over to 6-deoxyadenosylpterin, presumably by radical addition of the 5'-deoxyadenosine followed by oxidative decarboxylation to the product. In the absence of the strong reductant, dithionite, the carboxylate of 6-carboxypterin is esterified to generate 6-carboxypterin-5'-deoxyadenosyl ester | Bacillus subtilis 168 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CDG synthase | - |
Bacillus subtilis |
queE | - |
Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
4Fe-4S-center | S-adenosyl-L-methionine binds to the unique iron atom of a site-differentiated [4Fe-4S] cluster and is reductively cleaved to generate a 5'-deoxyadenosyl radical, which initiates turnover | Bacillus subtilis | |
S-adenosyl-L-methionine | S-adenosyl-L-methionine-dependent radical enzyme | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme catalyzes a key step in the biosynthesis of 7-deazapurine containing natural products | Bacillus subtilis |