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Literature summary extracted from

  • Groce, S.L.; Lipscomb, J.D.
    Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates (2005), Biochemistry, 44, 7175-7188.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.15 wild-type and mutant enzymes expressed in Escherichia coli Brevibacterium fuscum

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.15 H200A Km-value for 3,4-dihydroxyphenylacetate is 6fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 33.3fold lower than wild-type value Brevibacterium fuscum
1.13.11.15 H200E Km-value for 3,4-dihydroxyphenylacetate is 75fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 11.1fold lower than wild-type value Brevibacterium fuscum
1.13.11.15 H200F Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 47.6fold lower than wild-type value Brevibacterium fuscum
1.13.11.15 H200N Km-value for 3,4-dihydroxyphenylacetate is 3fold lower than wild-type value, kcat for 3,4-dihydroxyphenylacetate is 3.33fold lower than wild-type value Brevibacterium fuscum
1.13.11.15 H200Q Km-value for 3,4-dihydroxyphenylacetate is similar to wild-type value, kcat for 3,4-dihydroxyphenylacetate is 2.5fold lower than wild-type value Brevibacterium fuscum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.15 0.0004
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200E Brevibacterium fuscum
1.13.11.15 0.005
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200A Brevibacterium fuscum
1.13.11.15 0.01
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H20N Brevibacterium fuscum
1.13.11.15 0.028
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200Q Brevibacterium fuscum
1.13.11.15 0.03
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, wild-type enzyme Brevibacterium fuscum
1.13.11.15 0.031
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200F Brevibacterium fuscum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.15 Fe contains an active site Fe(II) 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 3,4-dihydroxyphenylacetate + O2 proximal extradiol cleavage of the aromatic ring of the substrate Brevibacterium fuscum 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.15 2,3-HPCD
-
 Brevibacterium fuscum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.15 0.21
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200F Brevibacterium fuscum
1.13.11.15 0.3
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200A Brevibacterium fuscum
1.13.11.15 0.9
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200E Brevibacterium fuscum
1.13.11.15 3
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H20N Brevibacterium fuscum
1.13.11.15 4
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, mutant enzyme H200Q Brevibacterium fuscum
1.13.11.15 10
-
 3,4-Dihydroxyphenylacetate 24°C, pH 7.5, wild-type enzyme Brevibacterium fuscum