A glycyl radical solution: oxygen-dependent interconversion of pyruvate formate-lyase
نویسندگان
چکیده
منابع مشابه
Pyruvate formate-lyase mechanism involving the protein-based glycyl radical.
Pyruvate formate-lyase (also called formate acetyltransferase; EC 2.3.1.54; PFI .) catalyses the thiolytic cleavage of pyruvate by CoA, yielding acetyl-CoA and formate. This reaction is the key step in the glucose-fermentation route in Escherichziz coli and various other bacteria. Operationally, it resembles the (B-keto)thiolase reaction of the fatty-acid degradation cycle. The mechanism of pyr...
متن کاملPyruvate formate-lyase activating enzyme: elucidation of a novel mechanism for glycyl radical formation.
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](...
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)...
متن کاملThe glycyl radical enzyme TdcE can replace pyruvate formate-lyase in glucose fermentation.
Mutants of Escherichia coli unable to synthesize a functional pyruvate formate-lyase (PFL) are severely impaired in their capacity to grow by glucose fermentation. In a functional complementation assay designed to isolate the pfl gene from Clostridium butyricum, we fortuitously identified a gene that did not encode a PFL but nonetheless was able to complement the phenotypic defects caused by an...
متن کاملStructural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
Pyruvate formate-lyase activating enzyme generates a stable and catalytically essential glycyl radical on G(734) of pyruvate formate-lyase via the direct, stereospecific abstraction of a hydrogen atom from pyruvate formate-lyase. The activase performs this remarkable feat by using an iron-sulfur cluster and S-adenosylmethionine (AdoMet), thus placing it among the AdoMet radical superfamily of e...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 1998
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.1998.00941.x