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Literature summary extracted from

  • Di Giuro, C.M.; Konstantinovics, C.; Rinner, U.; Nowikow, C.; Leitner, E.; Straganz, G.D.
    Chiral hydroxylation at the mononuclear nonheme Fe(II) center of 4-(S) hydroxymandelate synthase - a structure-activity relationship analysis (2013), PLoS ONE, 8, e68932.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.46 expression of C-terminally strep-tagged enzyme in Escherichia coli strain BL21(DE3) Streptomyces coelicolor

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.46 additional information
-
 additional information steady-state kinetic analysis, overview Streptomyces coelicolor
1.13.11.46 0.035
-
 2-oxo-4-phenylbutanoic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.16
-
 4-methoxyphenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.22
-
 4-hydroxyphenylpyruvate pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.353
-
 phenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.46 Fe2+ a nonheme Fe(II) dependent dioxygenase Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.46 4-hydroxyphenylpyruvate + O2 Streptomyces coelicolor
-
 4-hydroxymandelate + CO2
-
 ?
1.13.11.46 4-hydroxyphenylpyruvate + O2 Streptomyces coelicolor A3(2)
-
 4-hydroxymandelate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.46 Streptomyces coelicolor
-
-
-
1.13.11.46 Streptomyces coelicolor A3(2)
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.46 recombinant C-terminally strep-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.46 2-oxo-4-phenylbutanoic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
1.13.11.46 2-oxo-4-phenylbutanoic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
1.13.11.46 4-fluorophenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
1.13.11.46 4-fluorophenylpyruvic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
1.13.11.46 4-hydroxyphenylpyruvate + O2
-
 Streptomyces coelicolor 4-hydroxymandelate + CO2
-
 ?
1.13.11.46 4-hydroxyphenylpyruvate + O2
-
 Streptomyces coelicolor A3(2) 4-hydroxymandelate + CO2
-
 ?
1.13.11.46 4-methoxyphenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
1.13.11.46 4-methoxyphenylpyruvic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
1.13.11.46 4-methylphenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
1.13.11.46 4-nitrophenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
1.13.11.46 additional information substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview Streptomyces coelicolor ?
-
 ?
1.13.11.46 additional information substrate specificity, overview, Hms accepts a range of 2-oxo acids, whereby the presence of an aromatic substituent is crucial for efficient substrate turnover. A hydrophobic substrate binding pocket is identified as the likely determinant of substrate specificity. The enzyme shows high regioselectivity of oxygenation and a strong coupling efficiency of C-C bond cleavage and subsequent hydroxylation. The turnover number of Hms strongly correlates with substrate hydrophobicity. Quantitative structure activity relationship and in silico docking analyses, e.g. with (S)-mandelate and (R)-mandelate, overview Streptomyces coelicolor A3(2) ?
-
 ?
1.13.11.46 phenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.46 (S)-hydroxymandelate synthase
-
 Streptomyces coelicolor
1.13.11.46 4-(S) hydroxymandelate synthase
-
 Streptomyces coelicolor
1.13.11.46 HMS
-
 Streptomyces coelicolor

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.46 25
-
 assay at Streptomyces coelicolor

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.13.11.46 0.035
-
 4-nitrophenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.077
-
 4-fluorophenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.13
-
 4-methylphenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.17
-
 2-oxo-4-phenylbutanoic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.88
-
 phenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 0.96
-
 4-methoxyphenylpyruvic acid pH 7.5, 25°C Streptomyces coelicolor
1.13.11.46 4.5
-
 4-hydroxyphenylpyruvate pH 7.5, 25°C Streptomyces coelicolor

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.46 7.5
-
 assay at Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
1.13.11.46 malfunction upon introduction of a steric barrier, which is suspected to obstruct the accommodation of the aromatic ring in the hydrophobic pocket during the final hydroxylation step, the racemization of product is obtained Streptomyces coelicolor