Pyruvate formate-lyase (PFL): literature review, structure analysis and suggestions for experiments. Version 2
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PFL_summary-suggestions_05-2012.pdf
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Created: 8th May 2012 at 13:38
Last updated: 8th Nov 2017 at 15:21
Last used: 17th Feb 2020 at 23:49
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Related items
Projects: SysMO-LAB
Institutions: Heidelberg Institute for Theoretical Studies (HITS gGmbH)
Comparative Systems Biology: Lactic Acid Bacteria
Programme: SysMO
Public web page: http://www.sysmo.net/index.php?index=57
Pyruvate formate-lyase (PFL) is an important enzyme in the metabolic pathway of lactic acid bacteria (LAB) and is held responsible for the regulation of the shift between homolactic acid to mixed acid fermentation. PFL catalysis the reversible reaction of acetyl-CoA and formate into pyruvate and CoA. A glycyl radical, who is regenerated within the reaction, is involved; therefore, PFL works only under strictly anaerobic conditions. For its activation, the C-terminal domain has to bind to the
...
Person responsible: Stefan Henrich
Snapshots: No snapshots
Pyruvate formate-lyase (PFL) is an important enzyme in the metabolic pathway of lactic acid bacteria (LAB) and is held responsible for the regulation of the shift between homolactic acid to mixed acid fermentation. PFL catalysis the reversible reaction of acetyl-CoA and formate into pyruvate and CoA. A glycyl radical, who is regenerated within the reaction, is involved; therefore, PFL works only under strictly anaerobic conditions. For its activation, the C-terminal domain has to bind to the
...
Contributor: Stefan Henrich
Biological problem addressed: Model Analysis Type
Snapshots: No snapshots
