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Literature summary extracted from

  • Groce, S.L.; Lipscomb, J.D.
    Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme (2003), J. Am. Chem. Soc., 125, 11780-11781.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.15 H200F switch of reaction from extradiol to intradiol cleavage for substrate 2,3-dihydroxybenzoate Brevibacterium fuscum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.15 Fe2+
-
Brevibacterium fuscum

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.15 Brevibacterium fuscum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.15 2,3-dihydroxybenzoate + O2
-
Brevibacterium fuscum CO2 + alpha-hydroxymuconic semialdehyde mutant H200F produces alpha-carboxy-cis,cis-muconic acid ?
1.13.11.15 3,4-dihydroxyphenylacetate + O2
-
Brevibacterium fuscum 2-hydroxy-5-carboxymethyl-cis,cis-muconate semialdehyde
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.15 0.01
-
2,3-Dihydroxybenzoate mutant H200F Brevibacterium fuscum
1.13.11.15 0.02
-
2,3-Dihydroxybenzoate wild-type Brevibacterium fuscum
1.13.11.15 0.12
-
3,4-Dihydroxyphenylacetate mutant H200F Brevibacterium fuscum
1.13.11.15 10
-
3,4-Dihydroxyphenylacetate wild-type Brevibacterium fuscum