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Literature summary extracted from

  • Orenes-Pinero, E.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
    A new process for obtaining hydroxytyrosol using transformed Escherichia coli whole cells with phenol hydroxylase gene from Geobacillus thermoglucosidasius (2013), Food Chem., 139, 377-383.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.14.14.20 synthesis phenol hydroxylase gene cloning from the thermophilic bacteria Geobacillus thermoglucosidasius is used to develop an effective method to convert tyrosol into the high-added-value compound hydroxytyrosol by hydroxylation Parageobacillus thermoglucosidasius

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.20 gene pheA1, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli, cloning of the pheA1 promoter from Geobacillus thermoglucosidasius and use for enzyme expression in Escherichia coli strain Rosetta, tandem expression of genes pheA1 and pheA2 Parageobacillus thermoglucosidasius
1.14.14.20 gene pheA2, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain Rosetta tandem expression of genes pheA1 and pheA2 Parageobacillus thermoglucosidasius

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.20 additional information optimisation of conditions for diphenol and hydroxytyrosol production by transformed Escherichia coli cells Parageobacillus thermoglucosidasius

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.20 17800
-
2 * 17800, PheA2, about, sequence calculation Parageobacillus thermoglucosidasius
1.14.14.20 57000
-
2 * 57000, SDS-PAGE Parageobacillus thermoglucosidasius

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.20 phenol + FADH2 + O2 Parageobacillus thermoglucosidasius
-
catechol + FAD + H2O
-
?
1.14.14.20 phenol + FADH2 + O2 Parageobacillus thermoglucosidasius A7
-
catechol + FAD + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.20 Parageobacillus thermoglucosidasius Q9LAG2 PheA2; gene pheA2
-
1.14.14.20 Parageobacillus thermoglucosidasius Q9LAG3 PheA1; gene pheA1
-
1.14.14.20 Parageobacillus thermoglucosidasius A7 Q9LAG2 PheA2; gene pheA2
-
1.14.14.20 Parageobacillus thermoglucosidasius A7 Q9LAG3 PheA1; gene pheA1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.20 phenol + FADH2 + O2
-
Parageobacillus thermoglucosidasius catechol + FAD + H2O
-
?
1.14.14.20 phenol + FADH2 + O2
-
Parageobacillus thermoglucosidasius A7 catechol + FAD + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.20 homodimer 2 * 57000, SDS-PAGE Parageobacillus thermoglucosidasius
1.14.14.20 homodimer 2 * 17800, PheA2, about, sequence calculation Parageobacillus thermoglucosidasius
1.14.14.20 More the large subunit of this enzyme is encoded by pheA1 gene and gives rise to a 57 kDa protein. The protein has hydroxylase activity, is a homodimer, but has no activity by its own Parageobacillus thermoglucosidasius
1.14.14.20 More the minor component encoded by pheA2 gene has a predicted molecular mass of 17.8 kDa, it is a homodimer and shows a specific NADH:FAD reductase activity Parageobacillus thermoglucosidasius

Synonyms

EC Number Synonyms Comment Organism
1.14.14.20 PheA1
-
Parageobacillus thermoglucosidasius
1.14.14.20 PheA2
-
Parageobacillus thermoglucosidasius

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.20 FADH2
-
Parageobacillus thermoglucosidasius

General Information

EC Number General Information Comment Organism
1.14.14.20 physiological function phenol hydroxylase is a two-component enzyme encoded by pheA1 and pheA2 genes and strictly dependent on NADH and FAD. The intracellular enzyme is a clear example of a two-component tetrameric flavoprotein hydroxylase, in which flavin reduction and substrate oxygenation take place in the same protein Parageobacillus thermoglucosidasius