O4878
Oxaloacetate Decarboxylase from Pseudomonas sp.
lyophilized powder, ≥100 units/mg solid
Sinónimos:
OAD
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
form
lyophilized powder
specific activity
≥100 units/mg solid
storage temp.
−20°C
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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.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Los clientes también vieron
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)
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
Monica Balsera et al.
The Journal of biological chemistry, 286(11), 9457-9467 (2011-01-07)
The oxaloacetate decarboxylase primary Na(+) pump (OAD) is an essential membrane protein complex that functions in the citrate fermentation pathway of some pathogenic bacteria under anaerobic conditions. OAD contains three different subunits: Oad-α, a biotinylated extrinsic protein that catalyzes the
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
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