EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.20.15 | Fe2+ | the chloroferryl intermediate state of the enzyme presents opportunities for structural characterization | Pseudomonas syringae pv. syringae |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | Pseudomonas syringae pv. syringae | the enzyme participates in syringomycin E biosynthesis | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? | |
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | Pseudomonas syringae pv. syringae B301D | the enzyme participates in syringomycin E biosynthesis | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.20.15 | Pseudomonas syringae pv. syringae | Q9RBY6 | - |
- |
1.14.20.15 | Pseudomonas syringae pv. syringae B301D | Q9RBY6 | - |
- |
6.2.1.70 | Pseudomonas syringae pv. syringae | Q52400 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | the enzyme participates in syringomycin E biosynthesis | Pseudomonas syringae pv. syringae | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? | |
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | the substrate consists of L-Thr tethered via thioester linkage to a covalently bound phosphopantetheine cofactor of a carrier protein, SyrB1. Without an appended amino acid, SyrB1 does not trigger formation of the chloroferryl intermediate state in SyrB2, even in the presence of free L-Thr or its analogues, but SyrB1 charged either by L-Thr or by any of several non-native amino acids does trigger the reaction by as much as 8000fold (for L-Thr-S-SyrB1). Triggering efficacy is sensitive to the structures of both the amino acid and the carrier protein, being diminished by 5-20fold when the native L-Thr is replaced by another amino acid and by about 40fold when SyrB1 is replaced by a heterologous carrier protein, CytC2. The SyrB2 chloroferryl state exhibits unprecedented stability (t1/2 = 30-110 min at 0°C), can be trapped in high concentration and purity by manual freezing without a cryosolvent, and represents an ideal target for structural characterization | Pseudomonas syringae pv. syringae | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? | |
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | the enzyme participates in syringomycin E biosynthesis | Pseudomonas syringae pv. syringae B301D | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? | |
1.14.20.15 | L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl- | the substrate consists of L-Thr tethered via thioester linkage to a covalently bound phosphopantetheine cofactor of a carrier protein, SyrB1. Without an appended amino acid, SyrB1 does not trigger formation of the chloroferryl intermediate state in SyrB2, even in the presence of free L-Thr or its analogues, but SyrB1 charged either by L-Thr or by any of several non-native amino acids does trigger the reaction by as much as 8000fold (for L-Thr-S-SyrB1). Triggering efficacy is sensitive to the structures of both the amino acid and the carrier protein, being diminished by 5-20fold when the native L-Thr is replaced by another amino acid and by about 40fold when SyrB1 is replaced by a heterologous carrier protein, CytC2. The SyrB2 chloroferryl state exhibits unprecedented stability (t1/2 = 30-110 min at 0°C), can be trapped in high concentration and purity by manual freezing without a cryosolvent, and represents an ideal target for structural characterization | Pseudomonas syringae pv. syringae B301D | 4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O | - |
? | |
6.2.1.70 | ATP + L-threonine + holo-[L-threonyl-carrier protein] | - |
Pseudomonas syringae pv. syringae | AMP + diphosphate + L-threonyl-[L-threonyl-carrier protein] | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.20.15 | SyrB2 | - |
Pseudomonas syringae pv. syringae |
6.2.1.70 | syrB1 | - |
Pseudomonas syringae pv. syringae |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.20.15 | metabolism | the enzyme participates in syringomycin E biosynthesis | Pseudomonas syringae pv. syringae |
6.2.1.70 | physiological function | L-Thr-charged SyrB1 is the native substrate of SyrB2. Without an appended amino acid, SyrB1 does not trigger formation of the chloroferryl intermediate state in SyrB2. SyrB1 charged either by L-Thr or by any of several non-native amino acids does trigger the reaction by as much as 8000fold (for L-Thr-S-SyrB1). Triggering efficacy is sensitive to the structures of both the amino acid and the carrier protein, being diminished by 5-20fold when the native L-Thr is replaced by another amino acid and by about 40-fold when SyrB1 is replaced by a heterologous carrier protein, CytC2 | Pseudomonas syringae pv. syringae |