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Literature summary for 1.13.11.15 extracted from
- Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum (1997), Protein Expr. Purif., 10, 1-9.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression in Escherichia coli | Brevibacterium fuscum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | triple mutant in which the three gaps in the sequence are removed does not show a significant change in metal content | Brevibacterium fuscum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.011 | - |
3,4-Dihydroxyphenylacetate | recombinant enzyme | Brevibacterium fuscum |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | recombinant enzyme contains 2.8 mol of iron per mol of enzyme | Brevibacterium fuscum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,4-dihydroxyphenylacetate + O2 | Brevibacterium fuscum | key ring cleavage step in metabolism of 3,4-dihydroxyphenylacetate | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brevibacterium fuscum | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 6.2 | - |
recombinant enzyme | Brevibacterium fuscum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3,4-dihydroxyphenylacetate + O2 | - |
Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? | |
| 3,4-dihydroxyphenylacetate + O2 | key ring cleavage step in metabolism of 3,4-dihydroxyphenylacetate | Brevibacterium fuscum | 2-hydroxy-5-carboxymethylmuconate semialdehyde | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | turnover-numbers of recombinant wild-type enzyme and mutant enzyme | Brevibacterium fuscum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
recombinant wild-type enzyme and mutant enzyme | Brevibacterium fuscum |
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