Pregled bibliografske jedinice broj: 392117
A Comparison of Reactivity of Natural Substrate Pyruvate and of the Inhibitor Oxamate in Pyuvate Formate-Lyase
A Comparison of Reactivity of Natural Substrate Pyruvate and of the Inhibitor Oxamate in Pyuvate Formate-Lyase // WATOC 2008 Abstracts (Poster Session 3)
Sydney, 2008. (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 392117 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
A Comparison of Reactivity of Natural Substrate Pyruvate and of the Inhibitor Oxamate in Pyuvate Formate-Lyase
Autori
Čondić-Jurkić, Karmen ; Zipse, Hendrik ; Smith, David M.
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
WATOC 2008 Abstracts (Poster Session 3)
/ - Sydney, 2008
Skup
The World Association of Theoretical and Computational Chemists (WATOC) 2008
Mjesto i datum
Sydney, Australija, 14.09.2008. - 19.09.2008
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
QM/MM; model; Pyruvate Formate-Lyase; pyruvate; oxamate
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
098-0982933-2937 - Računalno proučavanje strukture i funkcije proteina (Smith, David Matthew, MZOS ) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
