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- W2011841810 abstract "Porphobilinogen synthase (PBGS) catalyzes the first common reaction in the biosynthesis of the tetrapyrroles, the asymmetric condensation of two molecules of δ-aminolevulinic acid to form porphobilinogen. There is a variable requirement for an essential active site zinc that necessitates consideration of PBGS as an enzyme that may exhibit phylogenetic diversity in its chemical reaction mechanism. Recent crystal structures suggest reaction mechanisms that involve two covalent Schiff base linkages between adjacent active site lysine residues and each of the two substrate molecules. The reaction appears to stall at a covalently bound almost-product intermediate that is poised for breakdown to product upon binding of a substrate molecule to an adjacent active site and a subsequent conformational change." @default.
- W2011841810 created "2016-06-24" @default.
- W2011841810 creator A5081576631 @default.
- W2011841810 date "2004-10-01" @default.
- W2011841810 modified "2023-10-03" @default.
- W2011841810 title "The porphobilinogen synthase catalyzed reaction mechanism" @default.
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- W2011841810 doi "https://doi.org/10.1016/j.bioorg.2004.05.010" @default.
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