EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.99.53 | - |
Serratia marcescens |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.99.53 | calculation of solution structure. Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ ions show binding to an interaction site located between His28 and His114 | Serratia marcescens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.53 | cyanide | mimic of molecular oxygen, binds to the metal ion only | Serratia marcescens |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.53 | Cu2+ | Kd value 55 nM, from isothermal titration calorimetry, and for Cu1+, Kd value 1 nM from the experimentally determined redox potential | Serratia marcescens | |
1.14.99.53 | additional information | residues His28 and His114 in the catalytic center bind a variety of divalent metal ions such as Ca2+, Mg2+, Fe3+, Co2+, Zn2+, or Cu2+ with a clear preference for Cu2+ | Serratia marcescens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.99.53 | Serratia marcescens | O83009 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.99.53 | chitin + acceptor + O2 | - |
Serratia marcescens | ? + reduced acceptor + H2O | - |
? | |
1.14.99.53 | additional information | mechanistic model, copper is reduced on the enzyme by an externally provided electron and followed by oxygen binding and activation by internal electron transfer. Substrate binding involves an extended planar binding surface, including the metal binding site. Chitin binding protects two regions from 2H/1H exchange, Gln53-Ser58 and Leu110-Thr116 | Serratia marcescens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.99.53 | CBP21 | - |
Serratia marcescens |