A Comparison of Reactivity of Natural Substrate Pyruvate and of the Inhibitor Oxamate in Pyuvate Formate-Lyase (CROSBI ID 547429)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa
Podaci o odgovornosti
Čondić-Jurkić, Karmen ; Zipse, Hendrik ; Smith, David M.
engleski
A Comparison of Reactivity of Natural Substrate Pyruvate and of the Inhibitor Oxamate in Pyuvate Formate-Lyase
DFT and high-level quantum mechanical calculations have been performed on small model systems relevant to the substrate mechanism of Pyruvate Formate-Lyase (PFL), comparing the reactivity of the natural substrate pyruvate with that of the known inhibitor oxamate. For both substrates the presently accepted (consensus) mechanism, involving the addition of a cysteine-based thiyl radical to the carbonyl carbon of the substrate, is compared to an alternative mechanism involving hydrogen abstraction as the primary step. This mechanism, relevant because of the known structural homology between PFL and the ribonucleotide reductase family of enzymes.
QM/MM; model; Pyruvate Formate-Lyase; pyruvate; oxamate
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Podaci o prilogu
PP484-x.
2008.
objavljeno
Podaci o matičnoj publikaciji
WATOC 2008 Abstracts (Poster Session 3)
Sydney:
Podaci o skupu
The World Association of Theoretical and Computational Chemists (WATOC) 2008
poster
14.09.2008-19.09.2008
Sydney, Australija