PMID:10425676
| Citation |
Leppänen, VM, Merckel, MC, Ollis, DL, Wong, KK, Kozarich, JW and Goldman, A (1999) Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase. Structure 7:733-44 |
|---|---|
| Abstract |
Pyruvate formate lyase (PFL) catalyses a key step in Escherichia coli anaerobic glycolysis by converting pyruvate and CoA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate, involving an essential C alpha radical of Gly734 and two cysteine residues, Cys418 and Cys419, which may form thiyl radicals required for catalysis. We undertook this study to understand the structural basis for catalysis. |
| Links | |
| Keywords |
Acetyltransferases/chemistry; Amino Acid Sequence; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; Protein Conformation; Ribonucleotide Reductases/chemistry |
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