Any feedback?
Literature summary for 5.5.1.1 extracted from
- Structural basis for the substrate specificity and the absence of dehalogenation activity in 2-chloromuconate cycloisomerase from Rhodococcus opacus 1CP (2014), Biochim. Biophys. Acta, 1844, 1541-1549.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the crystallographic structure of the chloromuconate cycloisomerase from Rhodococcus opacus is determined at 2.5 A of resolution. Results highlight that a histidine, located in a loop that closes the active site cavity upon the binding of the substrate, could be related to the dehalogenation inability of Rho-2-CMCI | Rhodococcus opacus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus opacus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homooctamer | - |
Rhodococcus opacus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-chloromuconate cycloisomerase | - |
Rhodococcus opacus |
| Rho-2-CMCI | - |
Rhodococcus opacus |
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
