Röntgenstrukturanalyse der Pyruvat-Formiatlyase (PFL)

• Applicant: Dr. Wolfgang Kabsch
• Subject Area: Microbiology, Virology and Immunology
• Term: from 1999 to 2002
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 5177280

Pyruvate Formate lyase from E. coli is a radical enzyme that synthesizes Acetyl-CoA (and formate as co-product) from pyruvate and CoA. The reaction adopts a reversible radical mechanism to cleave the C1-C2-carbon bond of pyruvate in which a stable radical bound to Gly734 plays a crucial role. So far only one structure of a radical enzyme is known, ribonucleotide reductase class I, which contains a tyrosyl-radical stabilized by Fe(III) (Tyr122 of the R2-subunit). In contrast, the glycyl radical of PFL is stabilized only by the protein structure. Main goal of the proposed research is to determine the structure of PFL from E. coli which -- in conjunction with biochemical data -- is expected to reveal the enzyme mechanism at atomic detail.

• DFG Programme: Priority Programmes
• Subproject of: SPP 1071: Radikale in der enzymatischen Katalyse