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Literature summary for 1.14.14.9 extracted from

  • Prieto, M.A.; Perez-Aranda, A.; Garcia, J.L.
    Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range (1993), J. Bacteriol., 175, 2162-2167.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli K-12 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information W21, 4-hydroxyphenylacetate deficient mutant Escherichia coli

General Stability

General Stability Organism
rather unstable in solution Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
2 * 59000, SDS-PAGE 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 4-hydroxyphenylacetic acid degradative pathway 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
strain W, ATCC 11105 derived from ATCC 9637
-
no activity in Escherichia coli K-12
-
DH1 CECT 416, ATCC 27325
-

Purification (Commentary)

Purification (Comment) Organism
difficult because of the low stability of the enzyme in solution Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,5-dihydroxyphenylacetate + ? 155% of 4-hydroxyphenylacetate activity Escherichia coli ?
-
?
3,4-dihydroxyphenylacetate + ? 65% of 4-hydroxyphenylacetate Escherichia coli ?
-
?
3-hydroxyphenylacetate + NADH + O2 82% activity of 4-hydroxyphenylacetate Escherichia coli 3,4-hydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2
-
Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
4-hydroxyphenylacetate + NADH + O2 4-hydroxyphenylacetic acid degradative pathway Escherichia coli 3,4-dihydroxyphenylacetate + NAD+ + H2O
-
?
additional information rather broad substrate specificity, acting on mono- and dihydric phenols. Several substrates are below 50% of activity Escherichia coli ?
-
?
p-cresol + ? 51% of 4-hydroxyphenylacetate activity Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 59000, SDS-PAGE Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD no stimulation Escherichia coli
NADH dependent, not NADPH dependent Escherichia coli