O4878
Oxaloacetate Decarboxylase from Pseudomonas sp.
lyophilized powder, ≥100 units/mg solid
Synonyme(s) :
OAD
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
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Laissez-nous vous aiderNom du produit
Oxaloacetate Decarboxylase from Pseudomonas sp., lyophilized powder, ≥100 units/mg solid
form
lyophilized powder
specific activity
≥100 units/mg solid
storage temp.
−20°C
Quality Level
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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.
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.
Other Notes
One unit will convert 1.0 μmole of oxalacetate to pyruvate and CO2 per min at pH 8.0 at 25 °C.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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
Tomas Krupnik et al.
Molecular membrane biology, 28(7-8), 462-472 (2011-10-15)
GltS of Escherichia coli is a secondary transporter that catalyzes Na+-glutamate symport. The structural model of GltS shows two homologous domains with inverted membrane topology that are connected by a central loop that resides in the cytoplasm. Each domain contains
Oxalacetic carboxylase of Micrococcus lysodeikticus.
Herbert, D.
Methods in Enzymology, 1, 753-757 (1955)
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
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