Any feedback?
Literature summary for 1.14.99.53 extracted from
- Unfolding of CBP21, a lytic polysaccharide monooxygenase, without dissociation of its copper ion cofactor (2020), Biopolymers, 111, e23339.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| copper | Cu2+ does not dissociate from the protein molecule during unfolding | Serratia marcescens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Serratia marcescens | O83009 | cf. EC 1.14.99.54 | - |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| thermal unfolding of both apo- and holoCBP21 is reversible | Serratia marcescens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CBP21 | - |
Serratia marcescens |
| chitin-binding protein 21 | - |
Serratia marcescens |
| GbpA | - |
Serratia marcescens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal unfolding of both apo- and holoCBP21 is reversible. ApoCBP21 unfolds in a simple two-state transition manner. The peak temperature of the differential scanning calorimetry curve, tp, for holoCBP21is (74.4°C and that for apoCBP21 is 65.6°C). HoloCBP21 is stabilized by 35 kJ/mol in terms of the Gibbs energy change for unfolding (pH 5.0, 25°C), compared with apoCBP21 | Serratia marcescens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
