EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.11.15 | H200N | site-directed mutagenesis, catalytic reaction intermediate formation in the mutant differs from the wild-type enzyme, Mössbauer spectral analysis, overview | Brevibacterium fuscum |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.15 | Co2+ | - |
Brevibacterium fuscum | |
1.13.11.15 | Fe2+ | FeHPCD, substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites | Brevibacterium fuscum | |
1.13.11.15 | Mn2+ | MnHPCD | Brevibacterium fuscum | |
1.13.11.15 | additional information | the enzyme is fully functional using metals with a redox potential range spanning 1.15 V. Recombinant extradiol dioxygenase homoprotocatechuate 2,3-dioxygenase functions with the same kcat, and kcat/KmO2 values within error when the Fe2+ is replaced by Mn2+. It exhibits even higher kcat and KmO2 values when Co2+ is substituted | Brevibacterium fuscum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.15 | 3,4-dihydroxyphenylacetate + O2 | Brevibacterium fuscum | - |
2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.15 | Brevibacterium fuscum | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.15 | 3,4-dihydroxyphenylacetate + O2 | - |
Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? | |
1.13.11.15 | 3,4-dihydroxyphenylacetate + O2 | substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites. Transfer of an electron(s) from 3,4-dihydroxyphenylacetate to O2 via the iron is proposed to activate the substrates for reaction with each other to initiate aromatic ring cleavage. Oxygen is bound as a (hydro)peroxo ligand. At least four intermediates form following addition of O2 with a pre-formed enzyme-substrate complex, different intermediate formation in mutant H200N, Mössbauer spectral analysis, overview | Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.15 | FeHPCD | - |
Brevibacterium fuscum |
1.13.11.15 | homoprotocatechuate 2,3-dioxygenase | - |
Brevibacterium fuscum |
1.13.11.15 | MnHPCD | - |
Brevibacterium fuscum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.11.15 | 22 | - |
assay at room temperature | Brevibacterium fuscum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.11.15 | 7.5 | - |
assay at | Brevibacterium fuscum |