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  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. (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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-A4DE-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-6520-A
Genre: Journal Article

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GER049.pdf (Publisher version), 0B
 
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http://dx.doi.org/10.1046/j.1432-1327.2001.02262.x (Publisher version)
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 Creators:
Brock, M., Author
Darley, D., Author
Textor, S.1, Author           
Buckel, W., Author
Affiliations:
1Department of Biochemistry, MPI for Chemical Ecology, Max Planck Society, ou_421893              

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Free keywords: Aspergillus nidulans; Escherichia coli; propionate metabolism; methylisocitrate lyase; isocitrate lyase Isocitrate lyase; propionate; mutase; cycle
 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

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 Dates: 2001
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: GER049
DOI: 10.1046/j.1432-1327.2001.02262.x
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 268 (12) Sequence Number: - Start / End Page: 3577 - 3586 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040