Interactions of substrate and non-substrate effectors with p-hydroxybenzoate hydroxylase from psuedomonas fluorescens
نویسندگان
چکیده
منابع مشابه
On the stable enzyme-substrate complex of p-hydroxybenzoate hydroxylase. Evidences for the proton uptake from the substrate.
p-Hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas desmolytica is known to form a stable complex with its substrate. Investigations were made on properties of the complex by spectrophotometric measurements and photooxidation. The addition ofp-hydroxybenzoate or benzoate to the oxidized (with respect to bound FAD) enzyme solution caused changes in absorption, fluorescence, and CD spec...
متن کاملConformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: single-molecule studies.
p-Hydroxybenzoate hydroxylase (PHBH) is a homodimeric enzyme in which each subunit noncovalently binds one molecule of FAD in the active site. PHBH is a model system for how flavoenzymes regulate reactions with oxygen. We report single-molecule fluorescence studies of PHBH in the absence of substrate that provide data consistent with the hypothesis that a critical step in substrate binding is t...
متن کاملCrystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida.
1. The inducible p-hydroxybenzoate hydroxylase of Pseudomonas putidu which catalyzes the hydroxylation of P-hydroxybenzoate to protocatechuate has been obtained in crystalline form as a protein homogeneous upon ultracentrifugation and electrophoresis. The molecular weight is estimated to be 83,600. 2. The enzyme contains approximately 1 mole of flavin adenine dinucleotide per mole of protein. R...
متن کاملModelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase.
The simulation of enzymatic reactions, using computer models, is becoming a powerful tool in the most fundamental challenge in biochemistry: to relate the catalytic activity of enzymes to their structure. In the present study, various computed parameters were correlated with the natural logarithm of experimental rate constants for the hydroxylation of various substrate derivatives catalysed by ...
متن کاملKinetic studies on the enzyme-substrate complex formation of p-hydroxybenzoate hydroxylase by the stopped-flow method.
The spectrophotometric and spectrofiuorometric investigations of the enzyme-substrate complex formation of p-hydroxybenzoate hydroxylase was made by the stopped-flow technique. The apparent velocity of the formation of the enzyme-substrate complex (the velocity of the absorbance change in visible and UV regions, and the velocity of the quenching of the fluorescence intensity in the FAD moiety o...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 1971
ISSN: 0006-291X
DOI: 10.1016/0006-291x(71)90148-3