H9886
p-Hydroxybenzoate Hydroxylase from Pseudomonas sp.
lyophilized powder, ~20 units/mg solid
Synonym(s):
4-Hydroxybenzoate, NADPH:oxygen oxidoreductase (3-hydroxylating)
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
form
lyophilized powder
specific activity
~20 units/mg solid
mol wt
55-~60 kDa
color
yellow
storage temp.
−20°C
General description
Michaelis constants : 2.0 x 10-5M (p-Hydroxybenzoate), 4.0 x 10-5M (NADPH)
Structure : One mol of FAD per mol of enzyme
Inhibitors : Ag+, Hg++, PCMB, SDS
Optimum pH : 7.7 - 7.9
Optimum temperature : 35oC
pH Stability : pH 5.0 - 7.5 (25oC, 72hr)
Thermal stability : below 40oC (pH 6.0, 15min)
Structure : One mol of FAD per mol of enzyme
Inhibitors : Ag+, Hg++, PCMB, SDS
Optimum pH : 7.7 - 7.9
Optimum temperature : 35oC
pH Stability : pH 5.0 - 7.5 (25oC, 72hr)
Thermal stability : below 40oC (pH 6.0, 15min)
Application
This enzyme is useful for enzymatic determination of choline esterase when coupled with protocatechuate 3, 4-dioxygenase.
Physical form
Contains mannitol and stabilizers
Other Notes
One unit will hydroxylate 1.0 μmole of p-hydroxybenzoate to protocatechuate per min at pH 8.2 at 37 °C in the presence of NADPH.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
Product Information Sheet
High-accuracy computation of reaction barriers in enzymes.
Frederik Claeyssens et al.
Angewandte Chemie (International ed. in English), 45(41), 6856-6859 (2006-09-23)
David P Ballou et al.
Biochemical and biophysical research communications, 338(1), 590-598 (2005-10-21)
Flavoprotein monooxygenases are involved in a wide variety of biological processes including drug detoxification, biodegradation of aromatic compounds in the environment, biosynthesis of antibiotics and siderophores, and many others. The reactions use NAD(P)H and O2 as co-substrates and insert one
Lindsay J Cole et al.
Biochemistry, 44(45), 14807-14817 (2005-11-09)
p-Hydroxybenzoate hydroxylase is extensively studied as a model for single-component flavoprotein monooxygenases. It catalyzes a reaction in two parts: (1) reduction of the FAD in the enzyme by NADPH in response to binding of p-hydroxybenzoate to the enzyme and (2)