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Literature summary for 1.1.3.46 extracted from

  • Li, T.L.; Choroba, O.W.; Charles, E.H.; Sandercock, A.M.; Williams, D.H.; Spencer, J.B.
    Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics (2001), Chem. Commun. (Camb. ), 21, 1752-1753.
    View publication on PubMed
Search for more literature for 1.1.3.46

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Amycolatopsis orientalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39863
-
 x * 39863, electrospray ionization mass spectrometry Amycolatopsis orientalis
39864
-
 x * 39864, calculated from sequence Amycolatopsis orientalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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 (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate ?
(S)-3,5-dihydroxymandelate + O2 Amycolatopsis orientalis the enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics 2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Amycolatopsis orientalis G4V4S8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Amycolatopsis orientalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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 (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics Amycolatopsis orientalis 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate ?
(S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O2 (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate i.e. (S)-4-hydroxymandelate Amycolatopsis orientalis 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2 2-(4-hydroxyphenyl)-2-oxoacetate i.e. 4-hydroxyphenylglyoxylate ?
(S)-3,5-dihydroxymandelate + O2
-
 Amycolatopsis orientalis 2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
-
 ?
(S)-3,5-dihydroxymandelate + O2 the enzyme is involed in the biosynthesis of (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics Amycolatopsis orientalis 2-(3,5-dihydroxyphenyl)-2-oxoacetate + H2O2
-
 ?
(S)-mandelate + O2 no activity with (R)-mandelate Amycolatopsis orientalis 2-phenyl-2-oxoacetate + H2O2
-
 ?

Subunits

Subunits Comment Organism
? x * 39863, electrospray ionization mass spectrometry Amycolatopsis orientalis
? x * 39864, calculated from sequence Amycolatopsis orientalis

Synonyms

Synonyms Comment Organism
4HmO
-
 Amycolatopsis orientalis
HmO
-
 Amycolatopsis orientalis
hydroxymandelate oxidase
-
 Amycolatopsis orientalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Amycolatopsis orientalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Amycolatopsis orientalis

Cofactor

Cofactor Comment Organism Structure
FMN flavoprotein Amycolatopsis orientalis

General Information

General Information Comment Organism
physiological function the enzyme is involed in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics Amycolatopsis orientalis