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Literature summary extracted from

  • Hsu, S.K.; Lin, L.L.; Lo, H.H.; Hsu, W.H.
    Mutational analysis of feedback inhibition and catalytic sites of prephenate dehydratase from Corynebacterium glutamicum (2004), Arch. Microbiol., 181, 237-244.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.51 expression of the His-tagged wild-type and mutant enzymes in Escherichia coli JM109 Corynebacterium glutamicum

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.51 E64D constructed by PCR-based random mutagenesis and complementation analysis, 15% reduced activity compared to the wild-type enzyme, 4.5% increased Km, 1.7fold increased kcat Corynebacterium glutamicum
4.2.1.51 E64Q constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum
4.2.1.51 E64S constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum
4.2.1.51 E64V constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum
4.2.1.51 F185L constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum
4.2.1.51 F185Y constructed by PCR-based random mutagenesis and complementation analysis, 96% reduced activity compared to the wild-type enzyme, 26% increased Km Corynebacterium glutamicum
4.2.1.51 additional information alterations of Asp76, Glu89, His115, and Arg236 do not cause significant changes in the kinetics properties Corynebacterium glutamicum
4.2.1.51 R184L constructed by PCR-based random mutagenesis and complementation analysis, 50% reduced activity compared to the wild-type enzyme Corynebacterium glutamicum
4.2.1.51 S99A constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine Corynebacterium glutamicum
4.2.1.51 S99C constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine Corynebacterium glutamicum
4.2.1.51 S99L constructed by PCR-based random mutagenesis and complementation analysis, insensitive to inhibition by phenylalanine Corynebacterium glutamicum
4.2.1.51 S99M constructed by PCR-based random mutagenesis and complementation analysis, 30% reduced activity compared to the wild-type enzyme, insensitive to inhibition by phenylalanine Corynebacterium glutamicum
4.2.1.51 T183A constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum
4.2.1.51 T183S constructed by PCR-based random mutagenesis and complementation analysis, highly reduced activity Corynebacterium glutamicum
4.2.1.51 T183Y constructed by PCR-based random mutagenesis and complementation analysis, inactive mutant Corynebacterium glutamicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.51 L-phenylalanine feedback inhibition, Ser99 is involved, mutants S99M, S99T, S99A, S99C, or S99L are not sensitive to inhibition Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.51 0.07
-
 prephenate wild-type enzyme, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.08
-
 prephenate mutant S99T, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.09
-
 prephenate mutant S99C, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.13
-
 prephenate mutant S99A, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.18
-
 prephenate mutant S99M, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.29
-
 prephenate mutant E164D, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.46
-
 prephenate mutant T183S, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.61
-
 prephenate mutant R184L, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 1.73
-
 prephenate mutant F185Y, pH 7.5, 30°C Corynebacterium glutamicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.51 39000
-
 x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.51 prephenate Corynebacterium glutamicum enzyme is a key regulatory enzyme in the phenylalanine-specific pathway phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate Corynebacterium glutamicum CCRC 11384 enzyme is a key regulatory enzyme in the phenylalanine-specific pathway phenylpyruvate + H2O + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.51 Corynebacterium glutamicum
-
-
-
4.2.1.51 Corynebacterium glutamicum CCRC 11384
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.51 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli Corynebacterium glutamicum

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.51 prephenate = phenylpyruvate + H2O + CO2 this enzyme in the enteric bacteria also possesses chorismate mutase activity, EC 5.4.99.5, and converts chorismate into prephenate, residues Glu64, Thr183, Arg184, and Phe185 might be involved in catalysis and substrate binding Corynebacterium glutamicum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.51 0.32
-
 mutant F185Y, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.39
-
 mutant T183S, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 2.37
-
 mutant S99A, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 4.31
-
 mutant R184L, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 6.66
-
 mutant S99M, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 6.88
-
 mutant S99C, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 7.59
-
 mutant S99T, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 8.1
-
 mutant E164D, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 9.48
-
 wild-type enzyme, pH 7.5, 30°C Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.51 prephenate
-
 Corynebacterium glutamicum phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate enzyme is a key regulatory enzyme in the phenylalanine-specific pathway Corynebacterium glutamicum phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate
-
 Corynebacterium glutamicum CCRC 11384 phenylpyruvate + H2O + CO2
-
 ?
4.2.1.51 prephenate enzyme is a key regulatory enzyme in the phenylalanine-specific pathway Corynebacterium glutamicum CCRC 11384 phenylpyruvate + H2O + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.51 ? x * 39000, recombinant wild-type and mutant enzymes, SDS-PAGE Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.51 30
-
 assay at Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.51 0.01
-
 prephenate mutant F185Y, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.01
-
 prephenate mutant T183S, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.03
-
 prephenate mutant S99A, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.09
-
 prephenate mutant S99C, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.11
-
 prephenate mutant S99T, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.12
-
 prephenate mutant S99M, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.12
-
 prephenate wild-type enzyme, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.13
-
 prephenate mutant R184L, pH 7.5, 30°C Corynebacterium glutamicum
4.2.1.51 0.21
-
 prephenate mutant E164D, pH 7.5, 30°C Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.51 7.5
-
 assay at Corynebacterium glutamicum