Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity
| Autor: | Florence Mus, Gregory A. Prussia, George H. Gauss, John W. Peters, Jennifer L. DuBois, Leah Conner |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Stereochemistry Biophysics Coenzyme M Biochemistry Catalysis Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Structural Biology Oxidoreductase Catalytic Domain Xanthobacter Genetics Organic chemistry Molecular Biology chemistry.chemical_classification 030102 biochemistry & molecular biology biology Active site Ketone Oxidoreductases Cell Biology Dipeptides Carbon Dioxide Pyruvate carboxylase 030104 developmental biology Enzyme chemistry Carboxylation Electrophile biology.protein Protons |
| Zdroj: | FEBS letters. 590(17) |
| ISSN: | 1873-3468 |
| Popis: | 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 to discriminating between carbon dioxide and protons as attacking electrophiles. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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