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Literature summary for 6.4.1.4 extracted from
- An unanticipated architecture of the 750-kDa holoenzyme of 3-methylcrotonyl-CoA carboxylase (2012), Nature, 481, 219-223.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the alpha and beta subunits of PaMCC are co-expressed in Escherichia coli as His-tagged fusion proteins | Pseudomonas aeruginosa |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structures of the Pseudomonas aeruginosa MCC (PaMCC) holoenzyme, alone and in complex with coenzyme A are shown at 2.9 and 3.5 A resolution respectively. The structures show that the architecture and overall shape of PaMCC are strikingly different when compared to propionyl-CoA carboxylase | Pseudomonas aeruginosa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | Q9I299 and Q9I297 | Q9I299, alpha-subunit and Q9I297, beta-subunit | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PaMCC | - |
Pseudomonas aeruginosa |
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Release 2023.1 (January 2023)
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