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Literature summary for 2.3.1.262 extracted from

  • Hutter, M.C.; Brengel, C.; Negri, M.; Henn, C.; Zimmer, C.; Hartmann, R.W.; Empting, M.; Steinbach, A.
    Mechanistic details for anthraniloyl transfer in PqsD: the initial step in HHQ biosynthesis (2014), J. Mol. Model., 20, 2255.
    View publication on PubMed
Search for more literature for 2.3.1.262

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations reveal a nucleophilic attack of the deprotonated sulfur of residue Cys112 at the carbonyl carbon of anthraniloyl-coenzyme A and a switch in the protonation pattern of His257 whereby Ndelta is protonated and the proton of Nepsilon? is shifted to the sulfur of CoA during the reaction Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
C112A inactive Pseudomonas aeruginosa
C112S decrease in activity Pseudomonas aeruginosa
H257F inactive Pseudomonas aeruginosa
N287A inactive Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P20582
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anthraniloyl-CoA + L-cysteinyl-[PqsD protein]
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 Pseudomonas aeruginosa S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
-
 ?
additional information initial catalytic step of PqsD is the transfer of the anthraniloyl moiety to residue Cys112 under hydrolysis of the anthraniloyl-CoA thioester. The second step in the reaction that leads to Cys112-anthraniloyl and CoA is a concerted reaction mechanism. The deprotonated sulfur atom of Cys112 performs a nucleophilic attack at the carbonyl carbon of anthraniloyl-CoA while the proton at Nepsilon of His257 is simultaneously shifted to the sulfur atom of CoA. During the reaction, His257 switches its protonation pattern. Only Nepsilon is protonated in the reactant state, whereas the uptake of a proton at Ndelta to deprotonation of Cys112 leads to a doubly protonated (positively charged) intermediate. From there, the proton at Nepsilon is subsequently transferred to the sulfur of CoA, leading to a net neutral product Pseudomonas aeruginosa ?
-
 ?
S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA
-
 Pseudomonas aeruginosa 2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
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 ?