O4878
Oxaloacetate Decarboxylase from Pseudomonas sp.
lyophilized powder, ≥100 units/mg solid
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Synonym(s):
OAD
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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General description
Oxaloacetate decarboxylase or OAD functions as a Na pump in anaerobic bacteria. It is a membrane protein consisting of three subunits, α, β and γ with the α subunit containing the carboxylase activity.
Application
Oxaloacetate Decarboxylase from Pseudomonas sp. has been used in the digestion of the low molecular weight (LMW) human milk fraction (5kF fraction) and as a positive control for deciphering C. thermocellum oxaloacetate decarboxylase activity.
Oxaloacetate decarboxylase has been used in a study to assess turnover and accessibility of a reentrant loop of the Na(+)-glutamate transporter GltS. It has also been used in a study to investigate fermentation and metabolic characteristics of Gluconacetobacter oboediens for different carbon sources.
Biochem/physiol Actions
Oxaloacetate Decarboxylase catalyzes the decarboxylation of oxaloacetate and requires manganese and magnesium for its activity. It is associated with a wide vareity of Gram-negative bacteria.
Unit Definition
One unit will convert 1.0 μmole of oxalacetate to pyruvate and CO2 per min at pH 8.0 at 25 °C.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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N E Labrou et al.
Archives of biochemistry and biophysics, 365(1), 17-24 (1999-05-01)
Oxaloacetate decarboxylase (OXAD), the enzyme that catalyzes the decarboxylation of oxaloacetate to pyruvic acid and carbon dioxide, was purified 245-fold to homogeneity from Pseudomonas stutzeri. The three-step purification procedure comprised anion-exchange chromatography, metal-chelate affinity chromatography, and biomimetic-dye affinity chromatography. Estimates
Determining citrate in fruit juices using a biosensor with citrate lyase and oxaloacetate decarboxylase in a flow injection analysis system.
Kim, M.
Food Chemistry, 99(4), 851-857 (2006)
Pablo D Sender et al.
FEBS letters, 570(1-3), 217-222 (2004-07-15)
The citM gene from Lactococcus lactis CRL264 was demonstrated to encode for an oxaloacetate decarboxylase. The enzyme exhibits high levels of similarity to malic enzymes (MEs) from other organisms. CitM was expressed in Escherichia coli, purified and its oxaloacetate decarboxylase
Huafang Lai et al.
Applied and environmental microbiology, 72(12), 7785-7792 (2006-09-26)
Pyruvate carboxylase (PYC) is an ecologically, medically, and industrially important enzyme. It is widespread in all three domains of life, the archaea, bacteria, and eukarya. PYC catalyzes ATP-dependent carboxylation of pyruvate to oxaloacetate. Detailed structure-function studies of this enzyme have
Pius Dahinden et al.
The FEBS journal, 272(3), 846-855 (2005-01-27)
The oxaloacetate decarboxylase Na+ pumps OAD-1 and OAD-2 of Vibrio cholerae are composed of a peripheral alpha-subunit associated with two integral membrane-bound subunits (beta and gamma). The alpha-subunit contains the carboxyltransferase domain in its N-terminal portion and the biotin-binding domain
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