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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.230 molecular dynamics simulations suggest a nucleophilic attack of the deprotonated sulfur of Cys112 at the carbonyl carbon of ACoA 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. In the N287A mutant anthraniloyl remains covalently bound to C112, further supporting that N87 does not take part in the cleavage of anthraniloyl-CoA Pseudomonas aeruginosa
2.3.1.262 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

EC Number Protein Variants Comment Organism
2.3.1.230 C112A inactive Pseudomonas aeruginosa
2.3.1.230 C112S about 20% of wild-type activity Pseudomonas aeruginosa
2.3.1.230 H257F inactive Pseudomonas aeruginosa
2.3.1.230 N287A inactive, anthraniloyl remains covalently bound to C112, further supporting that N87 does not take part in the cleavage of anthraniloyl-CoA Pseudomonas aeruginosa
2.3.1.262 C112A inactive Pseudomonas aeruginosa
2.3.1.262 C112S decrease in activity Pseudomonas aeruginosa
2.3.1.262 H257F inactive Pseudomonas aeruginosa
2.3.1.262 N287A inactive Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.230 Pseudomonas aeruginosa P20582
-
-
2.3.1.262 Pseudomonas aeruginosa P20582
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.262 anthraniloyl-CoA + L-cysteinyl-[PqsD protein]
-
 Pseudomonas aeruginosa S-anthraniloyl-L-cysteinyl-[PqsD protein] + CoA
-
 ?
2.3.1.262 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 ?
-
 ?
2.3.1.262 S-anthraniloyl-L-cysteinyl-[PqsD protein] + malonyl-CoA
-
 Pseudomonas aeruginosa 2-aminobenzoylacetyl-CoA + CO2 + L-cysteinyl-[PqsD protein]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.230 PsqD
-
 Pseudomonas aeruginosa