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Literature summary for 1.13.11.46 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
Search for more literature for 1.13.11.46

Cloned(Commentary)

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-
Streptomyces coelicolor A3(2)
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-4-phenylbutanoic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
2-oxo-4-phenylbutanoic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
4-fluorophenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
4-fluorophenylpyruvic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
4-hydroxyphenylpyruvate + O2
-
 Streptomyces coelicolor 4-hydroxymandelate + CO2
-
 ?
4-hydroxyphenylpyruvate + O2
-
 Streptomyces coelicolor A3(2) 4-hydroxymandelate + CO2
-
 ?
4-methoxyphenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
4-methoxyphenylpyruvic acid + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
4-methylphenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
4-nitrophenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?
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 ?
-
 ?
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) ?
-
 ?
phenylpyruvic acid + O2
-
 Streptomyces coelicolor ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

General Information

General Information Comment Organism
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