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Literature summary for 1.14.14.9 extracted from

  • Cooper, R.A.; Skinner, M.A.
    Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli (1980), J. Bacteriol., 143, 302-306.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information creation of 4-hydroxyphenylacetate-negative mutants by minimal salt medium with ethylmethanesulfonate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2 Escherichia coli degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2 Escherichia coli B / ATCC 11303 degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2 Escherichia coli C degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli C
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.026
-
with 3-hydroxyphenylacetate as substrate Escherichia coli
0.028
-
with 4-hydroxyphenylacetate as substrate Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2 enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
ir
4-hydroxyphenylacetate + NADH + O2 degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2 enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis Escherichia coli B / ATCC 11303 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
ir
4-hydroxyphenylacetate + NADH + O2 degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway Escherichia coli B / ATCC 11303 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2 enzyme is induced by 4-hydroxyphenylacetate, no constitutive synthesis Escherichia coli C 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
ir
4-hydroxyphenylacetate + NADH + O2 degradation of 4-hydroxyphenylacetate by inducible meta-cleavage pathway Escherichia coli C 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
additional information 3- and 4-hydroxyphenylacetate are both catalyzed by 3- or 4-hydroxyphenylacetate hydroxylase by the same route with 3,4-dihydroxyphenylacetate as the first common intermediate, cells grown on one compound are fully induced for the catabolism of the other Escherichia coli ?
-
?
additional information 3- and 4-hydroxyphenylacetate are both catalyzed by 3- or 4-hydroxyphenylacetate hydroxylase by the same route with 3,4-dihydroxyphenylacetate as the first common intermediate, cells grown on one compound are fully induced for the catabolism of the other Escherichia coli B / ATCC 11303 ?
-
?
additional information 3- and 4-hydroxyphenylacetate are both catalyzed by 3- or 4-hydroxyphenylacetate hydroxylase by the same route with 3,4-dihydroxyphenylacetate as the first common intermediate, cells grown on one compound are fully induced for the catabolism of the other Escherichia coli C ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADH can not be replaced by NADPH Escherichia coli