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Literature summary extracted from

  • Eppink, M.H.M.; Schreuder, H.A.; Van Berkel, W.J.H.
    Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants (1998), J. Biol. Chem., 273, 21031-21039.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.2 crystallization of mutant enzymes H162R and R269T by hanging drop vapour diffusion method Pseudomonas fluorescens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.2 H162D no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 H162K less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH Pseudomonas fluorescens
1.14.13.2 H162N no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 H162R rather efficient enzyme with similar catalytic properties as wild-type enzyme Pseudomonas fluorescens
1.14.13.2 H162S no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 H162T no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 H162Y rather efficient enzyme with similar catalytic properties as wild-type enzyme Pseudomonas fluorescens
1.14.13.2 R269D no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 R269K rather efficient enzyme with similar catalytic properties as wild-type enzyme Pseudomonas fluorescens
1.14.13.2 R269N no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 R269S less efficient than wild-type enzyme due to a clear increase in the apparent Km-value for NADPH Pseudomonas fluorescens
1.14.13.2 R269T no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens
1.14.13.2 R269Y no reliable turnover rate due to impaired NADPH binding Pseudomonas fluorescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.2 diethyl dicarbonate inhibition of wild-type enzyme, no inhibition of mutant enzyme H162R Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.2 additional information
-
additional information Km value for NADPH above 0.5 mM: mutant enzymes R269D, R269T, R269N, R269Y, H162D, H162T, H162S, H162N Pseudomonas fluorescens
1.14.13.2 0.02
-
4-hydroxybenzoate wild-type enzyme Pseudomonas fluorescens
1.14.13.2 0.03
-
NADPH wild-type enzyme Pseudomonas fluorescens
1.14.13.2 0.03
-
4-hydroxybenzoate mutant enzyme H162R, H162Y, H162K, R269K, R269Y, R269N, R269S and R269T Pseudomonas fluorescens
1.14.13.2 0.04
-
4-hydroxybenzoate mutant enzyme H162N, H162S, H162T and H162D Pseudomonas fluorescens
1.14.13.2 0.05
-
NADPH mutant enzyme H162R Pseudomonas fluorescens
1.14.13.2 0.06
-
4-hydroxybenzoate mutant enzyme R269D Pseudomonas fluorescens
1.14.13.2 0.07
-
NADPH mutant enzyme H162Y and R269K Pseudomonas fluorescens
1.14.13.2 0.2
-
NADPH mutant enzyme H162K Pseudomonas fluorescens
1.14.13.2 0.32
-
NADPH mutant enzyme R269S Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.2 Pseudomonas fluorescens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.2
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.2 4-hydroxybenzoate + NADPH + O2
-
Pseudomonas fluorescens protocatechuate + NADP+ + H2O
-
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Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.2 additional information
-
additional information
-
Pseudomonas fluorescens