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Literature summary extracted from

  • Hubbard, B.K.; Thomas, M.G.; Walsh, C.T.
    Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics (2000), Chem. Biol., 7, 931-942.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.46 expression in Escherichia coli Amycolatopsis orientalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.46 (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 Amycolatopsis orientalis (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of the non-proteinogenic amino acid (S)-4-hydroxyphenylglycine a constituent of peptide antibiotics 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate ?
2.6.1.B17 (2S)-4-hydroxyphenylglycine + 4-hydroxyphenylpyruvate Amycolatopsis orientalis
-
4-hydroxybenzoylformate + L-tyrosine
-
r
2.6.1.B17 4-hydroxybenzoylformate + L-tyrosine Amycolatopsis orientalis biosynthetic direction (2S)-4-hydroxyphenylglycine + 4-hydroxyphenylpyruvate
-
r
2.6.1.B17 additional information Amycolatopsis orientalis no amino acceptors: D-4-hydroxyphenylglycine, glutamate, pyruvate, oxaloacetate ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.46 Amycolatopsis orientalis G4V4S8
-
-
2.6.1.B17 Amycolatopsis orientalis O52815 cf. EC 2.6.1.103
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.46
-
Amycolatopsis orientalis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.B17 4-hydroxybenzoylformate + L-tyrosine = (2S)-4-hydroxyphenylglycine + 4-hydroxyphenylpyruvate biosynthetic direction Amycolatopsis orientalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.46 (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate. The enzyme is involed in the biosynthesis of the non-proteinogenic amino acid (S)-4-hydroxyphenylglycine a constituent of peptide antibiotics Amycolatopsis orientalis 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate ?
2.6.1.B17 (2S)-4-hydroxyphenylglycine + 4-hydroxyphenylpyruvate
-
Amycolatopsis orientalis 4-hydroxybenzoylformate + L-tyrosine
-
r
2.6.1.B17 4-hydroxybenzoylformate + 3-chloro-L-tyrosine
-
Amycolatopsis orientalis L-4-hydroxyphenylglycine + 3-chloro-4-hydroxyphenylpyruvate
-
?
2.6.1.B17 4-hydroxybenzoylformate + L-phenylalanine
-
Amycolatopsis orientalis (2S)-4-hydroxyphenylglycine + phenylpyruvate
-
?
2.6.1.B17 4-hydroxybenzoylformate + L-tyrosine biosynthetic direction Amycolatopsis orientalis (2S)-4-hydroxyphenylglycine + 4-hydroxyphenylpyruvate
-
r
2.6.1.B17 benzoylformate + L-tyrosine
-
Amycolatopsis orientalis L-phenylalanine + 4-hydroxyphenylpyruvate
-
?
2.6.1.B17 additional information no amino acceptors: D-4-hydroxyphenylglycine, glutamate, pyruvate, oxaloacetate Amycolatopsis orientalis ?
-
?

Subunits

EC Number Subunits Comment Organism
2.6.1.B17 ? x * 47777, calculated Amycolatopsis orientalis

Synonyms

EC Number Synonyms Comment Organism
1.1.3.46 HmO
-
Amycolatopsis orientalis
1.1.3.46 p-hydroxymandelate oxidase
-
Amycolatopsis orientalis
2.6.1.B17 4-hydroxyphenylglycine transaminase
-
Amycolatopsis orientalis
2.6.1.B17 HpgT
-
Amycolatopsis orientalis
2.6.1.B17 p-hydroxyphenylglycine transaminase
-
Amycolatopsis orientalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.46 FMN
-
Amycolatopsis orientalis
2.6.1.B17 pyridoxal 5'-phosphate exogenous pyridoxal 5'-phosphate is required for catalytic activity Amycolatopsis orientalis

General Information

EC Number General Information Comment Organism
2.6.1.B17 physiological function enzyme is part of the chloroeremomycin biosynthetic cluster. Non-heme iron dioxygenase HmaS catalyzes the synthesis of L-4-hydroxymandelate from 4-hydroxyphenylpyruvate. The L-4-hydroxymandelate is subsequently converted to L-4-hydroxyphenylglycine via L-4-hydroxymandelate oxidase Hmo catalyzed conversion of L-4-hydroxymandelate to L-4-hydroxybenzoylformate followed by 4-hydroxyphenylglycine transaminase HpgT catalyzed transamination of 4-hydroxybenzoylformate to 4-hydroxyphenylglycine. The biosynthesis of L-4-hydroxyphenylglycine is proposed to be a catalytic cycle initiated by the production of 4-hydroxyphenylpyruvate Amycolatopsis orientalis