2-Methylisocitrate lyases from the bacterium Escherichia coli and the 
filamentous fungus Aspergillus nidulans - Characterization and comparison of 
both enzymes

Brock, M.; Darley, D.; Textor, S.; Buckel, W.

doi:10.1046/j.1432-1327.2001.02262.x

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2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans - Characterization and comparison of both enzymes

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Textor, S.
Department of Biochemistry, MPI for Chemical Ecology, Max Planck Society;

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http://dx.doi.org/10.1046/j.1432-1327.2001.02262.x
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Citation

Brock, M., Darley, D., Textor, S., & Buckel, W. (2001). 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans - Characterization and comparison of both enzymes. European Journal of Biochemistry, 268(12), 3577-3586. doi:10.1046/j.1432-1327.2001.02262.x.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-A4DE-4

Abstract

In Escherichia coli and Aspergillus nidulans, propionate is oxidized to pyruvate via the methylcitrate cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate is catalysed by 2-methylisocitrate lyase. The enzymes