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Literature summary for 1.14.20.15 extracted from

  • Matthews, M.L.; Krest, C.M.; Barr, E.W.; Vaillancourt, F.H.; Walsh, C.T.; Green, M.T.; Krebs, C.; Bollinger, J.M.
    Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2 (2009), Biochemistry, 48, 4331-4343 .
    View publication on PubMedView publication on EuropePMC
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the chloroferryl intermediate state of the enzyme presents opportunities for structural characterization Pseudomonas syringae pv. syringae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
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 ?
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
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 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae pv. syringae Q9RBY6
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Pseudomonas syringae pv. syringae B301D Q9RBY6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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
-
 ?
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
-
 ?
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
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 ?

Synonyms

Synonyms Comment Organism
SyrB2
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 Pseudomonas syringae pv. syringae

General Information

General Information Comment Organism
metabolism the enzyme participates in syringomycin E biosynthesis Pseudomonas syringae pv. syringae