Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | Fe2+-containing homoprotocatechuate 2,3-dioxygenase, FeHPCD, activates O2 to catalyze the aromatic ring opening of homoprotocatechuate | Brevibacterium fuscum | |
Mn2+ | can substitute for Fe2+ in catalysis | Brevibacterium fuscum | |
additional information | the enzyme requires Fe2+ for catalysis, but Mn2+ can be substituted (MnHPCD) with essentially no change in the steady-state kinetic parameters, spectral analysis, overview | Brevibacterium fuscum | |
NO | NO binding to a non-heme enzyme containing manganese allows examination of the factors governing the formation and detection of the MIII-O2.- species in all forms of th enzyme. NO, and presumably O2, binding is sensitive to both the nature of the catecholic substrate present and the nature of the active-site amino acid residue at position 200, spectral analysis, overview | Brevibacterium fuscum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4-dihydroxyphenylacetate + O2 | Brevibacterium fuscum | - |
2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacterium fuscum | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4-dihydroxyphenylacetate + O2 | - |
Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? | |
3,4-dihydroxyphenylacetate + O2 | Fe2+-containing homoprotocatechuate 2,3-dioxygenase, FeHPCD, activates O2 to catalyze the aromatic ring opening of homoprotocatechuate. O2 activation steps for extradiol dioxygenases, mechanism, overview | Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? |
Synonyms | Comment | Organism |
---|---|---|
FeHPCD | - |
Brevibacterium fuscum |
homoprotocatechuate 2,3-dioxygenase | - |
Brevibacterium fuscum |
MnHPCD | - |
Brevibacterium fuscum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Brevibacterium fuscum |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme requires Fe2+ for catalysis, but Mn2+ can be substituted (MnHPCD) with essentially no change in the steady-state kinetic parameters, spectral analysis, overview | Brevibacterium fuscum |