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Literature summary for 1.3.1.2 extracted from

  • Beaupre, B.A.; Forouzesh, D.C.; Butrin, A.; Liu, D.; Moran, G.R.
    Perturbing the movement of hydrogens to delineate and assign events in the reductive activation and turnover of porcine dihydropyrimidine dehydrogenase (2021), Biochemistry, 60, 1764-1775 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Sus scrofa

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant C671S, to 1.69 A resolution. The thymine substrate is positioned over the FMNH2 cofactor with the 6-methyne carbon 3.3 A from flavin N5 Sus scrofa

Protein Variants

Protein Variants Comment Organism
C671A mutation eliminates the proton-coupled electron transfer required to reduce pyrimidine substrates Sus scrofa
C671S variant exhibits both delineation of reductive activation into two phases at low pH values and exceptionally slow turnover with thymine Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa Q28943
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General Information

General Information Comment Organism
metabolism the rate of turnover is not controlled by the protonation state of the general acid, cysteine 671. The initial phase results in the accumulation of charge transfer absorption added to the binding difference spectrum for NADPH. The second phase results in reduction of one of the two flavins. The presumed activated form of the enzyme has the FMN cofactor reduced. Charge transfer arises from the proximity of the NADPH and FAD bases and the ensuing flavin is a result of rapid transfer of electrons to the FMN without accumulation of reduced forms of the FAD or Fe4-S4 centers. The slow rate of turnover of DPD is governed by the movement of a mobile structural feature that carries the C671 residue Sus scrofa