Bioinformatic Characterization of Glycyl Radical Enzyme-Associated Bacterial Microcompartments
نویسندگان
چکیده
منابع مشابه
In Vitro Characterization and Concerted Function of Three Core Enzymes of a Glycyl Radical Enzyme - Associated Bacterial Microcompartment
Many bacteria encode proteinaceous bacterial microcompartments (BMCs) that encapsulate sequential enzymatic reactions of diverse metabolic pathways. Well-characterized BMCs include carboxysomes for CO2-fixation, and propanediol- and ethanolamine-utilizing microcompartments that contain B12-dependent enzymes. Genes required to form BMCs are typically organized in gene clusters, which promoted th...
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Anaerobic degradation of the environmental pollutant toluene is initiated by the glycyl radical enzyme benzylsuccinate synthase (BSS), which catalyzes the radical addition of toluene to fumarate, forming benzylsuccinate. We have determined crystal structures of the catalytic α-subunit of BSS with its accessory subunits β and γ, which both bind a [4Fe-4S] cluster and are essential for BSS activi...
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Pyruvate formate lyase activating enzyme is a member of a novel superfamily of enzymes that utilize S-adenosylmethionine to initiate radical catalysis. This enzyme has been isolated with several different iron-sulfur clusters, but single turnover monitored by EPR has identified the [4Fe-4S](1+) cluster as the catalytically active cluster; this cluster is believed to be oxidized to the [4Fe-4S](...
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متن کاملStructure and mechanism of the glycyl radical enzyme pyruvate formate-lyase[6]
The enzyme pyruvate formate-lyase (PFL) catalyzes the reversible conversion of pyruvate and CoA into acetyl-CoA and formate, which has a central role in anaerobic glucose fermentation by E. coli cells and other bacteria [1]. PFL a 2 × 85 kDa homodimer is the first example of a radical enzyme where the spin was found to be located on the polypeptide backbone Cα-atom of a glycyl residue (Gly 734)...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2015
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.02587-15