Synthesis of Bisubstrate Inhibitors of Porphobilinogen Synthase from  Pseudomonas aeruginosa | Zendy

Gacond Sabine | Zendy; Frère Frederic | Zendy; Nentwich Merle | Zendy; Faurite JeanPhilippe | Zendy; FrankenbergDinkel Nicole | Zendy; Neier Reinhard | Zendy

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Synthesis of Bisubstrate Inhibitors of Porphobilinogen Synthase from Pseudomonas aeruginosa

Author(s) -

Gacond Sabine,

Frère Frederic,

Nentwich Merle,

Faurite JeanPhilippe,

FrankenbergDinkel Nicole,

Neier Reinhard

Publication year - 2007

Publication title -

chemistry and biodiversity

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.427

H-Index - 70

eISSN - 1612-1880

pISSN - 1612-1872

DOI - 10.1002/cbdv.200790024

Subject(s) - porphobilinogen , levulinic acid , porphobilinogen synthase , chemistry , dehydratase , enzyme , atp synthase , stereochemistry , biochemistry , molecule , active site , organic chemistry , catalysis

Porphobilinogen synthase (PBGS) synthesizes porphobilinogen 2 (PBG), the common precursor of all natural tetrapyrroles, through an asymmetric condensation of two molecules of 5‐aminolevulinic acid 1 (ALA). Symmetrically linked dimers 7 – 11 derived from levulinic acid 3 ( γ ‐oxovaleric acid) have been synthesized to mimic the assumed bisubstrate bound to the active site of the enzyme. Their inhibition potential was characterized by determination of the IC 50 and K i values using PBGS from Pseudomonas aeruginosa. The polarity and the size of the functional group linking the two levulinic acid 3 units have a strong influence on the inhibition behavior.

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