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Documentos Principais

O4878

Sigma-Aldrich

Oxaloacetate Decarboxylase from Pseudomonas sp.

lyophilized powder, ≥100 units/mg solid

Sinônimo(s):

OAD

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About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulário

lyophilized powder

Nível de qualidade

atividade específica

≥100 units/mg solid

temperatura de armazenamento

−20°C

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Descrição geral

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.

Aplicação

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.

Ações bioquímicas/fisiológicas

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.

Definição da unidade

One unit will convert 1.0 μmole of oxalacetate to pyruvate and CO2 per min at pH 8.0 at 25 °C.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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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
Y Augagneur et al.
Journal of applied microbiology, 104(1), 260-268 (2007-10-12)
Citrate metabolism generates metabolic energy through the generation of a membrane potential and a pH gradient. The purpose of this work was to study the influence of oxaloacetate decarboxylase in citrate metabolism and intracellular pH maintenance in relation to acidic
Buvaneswari C Narayanan et al.
Biochemistry, 47(1), 167-182 (2007-12-18)
Pseudomonas aeruginosa PA4872 was identified by sequence analysis as a structurally and functionally novel member of the PEP mutase/isocitrate lyase superfamily and therefore targeted for investigation. Substrate screens ruled out overlap with known catalytic functions of superfamily members. The crystal
Dayanidhi Sarkar et al.
Applied microbiology and biotechnology, 87(1), 127-136 (2010-03-02)
The metabolism of Gluconacetobacter oboediens was investigated in relation to different carbon sources for the continuous cultures at the dilution rate of 0.05 h(-1). The 13C-flux result implies the formation of metabolic recycles for the case of using glucose and
Pius Dahinden et al.
Archives of microbiology, 183(2), 121-129 (2005-01-14)
The oxaloacetate decarboxylase (OAD) Na(+) pump consists of subunits alpha, beta, and gamma, which are expressed from an oadGAB gene cluster present in various anaerobic bacteria. Vibrio cholerae has two copies of oad genes, which are termed oad-1 and oad-2.

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