Literature summary for 1.13.11.24 extracted from

Wang, W.J.; Wei, W.J.; Liao, R.Z.
Deciphering the chemoselectivity of nickel-dependent quercetin 2,4-dioxygenase (2018), Phys. Chem. Chem. Phys., 20, 15784-15794 .

Search for more literature for 1.13.11.24

Organism

Organism	UniProt	Comment	Textmining
Streptomyces sp. FLA	A2VA43	-	-

Synonyms

Synonyms	Comment	Organism
QueD	-	Streptomyces sp. FLA
quercetinase	-	Streptomyces sp. FLA

General Information

General Information	Comment	Organism
metabolism	the reaction takes place via three major steps: attack of the superoxide on the C2 of the substrate pyrone ring to generate a Ni(II)-peroxide intermediate, formation of the second C-O bond between C4 and the peroxide to produce a peroxide bridge, and simultaneous cleavage of the C2-C3, C3-C4, and O1-O2 bonds with the formation of 2-protocatechuoylphloroglucinol carboxylic acid and carbon monoxide. The third step is rate-limiting, with a barrier of 17.4 kcal/mol. For the second C-O bond formation, an alternative pathway is that the peroxide attacks the C3 of the substrate pyrone ring, leading to the formation of a four-membered ring intermediate, which then undergoes concerted C2-C3 and O1-O2 bond cleavages to produce an alpha-keto acid. This pathway is associated with a barrier of 30.6 kcal/mol. When Glu74 is protonated, the 2,3-dioxygenolytic pathway, however, has a lower barrier (21.8 kcal/mol) than the 2,4-dioxygenolytic pathway	Streptomyces sp. FLA

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Release 2023.1 (January 2023)