Literature summary for 2.3.1.230 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.

Search for more literature for 2.3.1.230

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	P20582	-	-

Synonyms

Synonyms	Comment	Organism
PsqD	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)