EC Number | Application | Comment | Organism |
---|---|---|---|
1.1.2.B5 | diagnostics | bioelectrochemical applications (an amperometric biosensor) in electrochemical devices, based on direct electron transfer reactions. Development of a biosensor to detect urinary L-fucose | Coprinopsis cinerea |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.2.B5 | expression in Pichia pastoris | Coprinopsis cinerea |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.1.2.B5 | 98000 | - |
SDS-PAGE | Coprinopsis cinerea |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.2.B5 | Coprinopsis cinerea | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.2.B5 | additional information | no activity toward common monosaccharides, such as D-glucose, D-fructose, and cellobiose | Coprinopsis cinerea | ? | - |
- |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.2.B5 | 6 | - |
optimum pH for theoxidation reaction of L-fucose, the electron is directly transferred from the PQQ domain to the electron acceptor. At 8.5 the electron is transferred via the cytochrome domain. This phenomenon indicates that inter-domain electron transfer (IET) is strongly dependent on pH | Coprinopsis cinerea |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.B5 | heme | quinohemoprotein | Coprinopsis cinerea | |
1.1.2.B5 | pyrroloquinoline quinone | pyrroloquinoline quinone-dependent enzyme. The enzyme binds to pyrroloquinoline quinone at a ratio of 1: 1 | Coprinopsis cinerea |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.1.2.B5 | Coprinopsis cinerea | calculated from sequence | - |
7.7 |