Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.13.11.15 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
Search for more literature for 1.13.11.15

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Brevibacterium fuscum

Organism

Organism UniProt Comment Textmining
Brevibacterium fuscum
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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