Any feedback?
Literature summary for 4.2.1.3 extracted from
- Identification of a multienzyme complex of the tricarboxylic acid cycle enzymes containing citrate synthase isoenzymes from pseudomonas aeruginosa (1996), Biochem. J., 313, 769-774.
No PubMed abstract available
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Pseudomonas aeruginosa | aconitase is part of a multienzyme complex of the tricarboxylic acid cycle. Individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
mutant PAC514 from strain 8602 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| citrate | - |
Pseudomonas aeruginosa | cis-aconitate + H2O | - |
? | |
| additional information | aconitase is part of a multienzyme complex of the tricarboxylic acid cycle. Individual enzyme activities of fumarase, malate dehydrogenase, citrate synthase, aconitase and isocitrate dehydrogenase can be used to reconstitute the complex | Pseudomonas aeruginosa | ? | - |
? | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
