O4878
Oxalacetat-Decarboxylase aus Pseudomonas sp.
lyophilized powder, ≥100 units/mg solid
Synonym(e):
OAD
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
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Allgemeine Beschreibung
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.
Anwendung
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. Wirkung
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.
Einheitendefinition
1 U setzt 1.0 μmol Oxalacetat zu Pyruvat und CO2 pro Minute um bei pH 8.0 und 25°C.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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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)
Oxaloacetate Decarboxylase fromPseudomonas stutzeri: Purification and Characterization
Labrou NE and Clonis YD
Archives of Biochemistry and Biophysics, 365(1), 17-24 (1999)
Pius Dahinden et al.
Archives of microbiology, 182(5), 414-420 (2004-10-19)
Archaeoglobus fulgidus harbors three consecutive and one distantly located gene with similarity to the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae (KpOadGAB). The water-soluble carboxyl transferase (AfOadA) and the biotin protein (AfOadC) were readily synthesized in Escherichia coli, but the
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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