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Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase [ 6 ]
| Content Provider | Semantic Scholar |
|---|---|
| Author | Becker, Andreas Fritz-Wolf, Karin Kabsch, Wolfgang Knappe, Joachim Schultz, Sabine Wagner, Adolf Fritz Volker |
| Copyright Year | 1999 |
| Abstract | 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) [2,3]. Biochemical studies revealed that the substrate conversion by PFL proceeds via a homolytic mechanism and occurs through two half-reactions involving an acetyl-enzyme intermediate ( E + pyruvate acetyl-E + formate; acetyl-E + CoA E + acetyl-CoA) [4]. In the active site two adjacent cysteinyl residues (Cys 418, Cys 419) play a central role in carrying the intermediary acetyl. Moreover, it has been proposed that a thiyl radical from one of these two cysteine residues would be generated by the glycyl radical and used to promote the homolytic substrate cleavage. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://hasyweb.desy.de/science/annual_reports/1999_report/part2/contrib/72/1348.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
