| Literature DB >> 27447465 |
Gregory A Prussia1, George H Gauss1, Florence Mus1, Leah Conner1, Jennifer L DuBois1, John W Peters1.
Abstract
The characteristic His-Glu catalytic dyad of the disulfide oxidoreductase (DSOR) family of enzymes is replaced in 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) by the residues Phe-His. 2-KPCC is the only known carboxylating member of the DSOR family and has replaced this dyad potentially to eliminate proton-donating groups at a key position in the active site. Substitution of the Phe-His by the canonical residues results in production of higher relative concentrations of acetone versus the natural product acetoacetate. The results indicate that these differences in 2-KPCC are key in discriminating between carbon dioxide and protons as attacking electrophiles.Entities:
Keywords: carboxylation; catalytic dyad; protonation
Mesh:
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Year: 2016 PMID: 27447465 DOI: 10.1002/1873-3468.12325
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124