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.
    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
Search for more literature for 1.13.11.15

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe contains an active site Fe(II) Brevibacterium fuscum

Organism

Organism UniProt Comment Textmining
Brevibacterium fuscum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydroxyphenylacetate + O2 proximal extradiol cleavage of the aromatic ring of the substrate Brevibacterium fuscum 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?

Synonyms

Synonyms Comment Organism
2,3-HPCD
-
 Brevibacterium fuscum

Turnover Number [1/s]

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