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A6680

Sigma-Aldrich

N-Acetylneuraminic Acid Aldolase from microorganisms

lyophilized powder, ≥20 units/mg protein (biuret)

Synonyme(s) :

N-Acetylneuraminate Pyruvate Lyase, N-Acetylneuraminic Acid Lyase, NANA Aldolase, Sialic Aldolase

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About This Item

Numéro CAS:
9027-60-5
Numéro de classification (Commission des enzymes):
4.1.3.3 (BRENDA, IUBMB)
Numéro Beilstein :
2697172
Numéro MDL:
MFCD00131656
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Forme

lyophilized powder

Niveau de qualité

200

Activité spécifique

≥20 units/mg protein (biuret)

Poids mol.

~98 kDa

Température de stockage

−20°C

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Application

This enzyme is useful for enzymatic determination of N-acetylneuraminic acid and sialic acid when
coupled with the related enzymes in clinical analysis.
For industrial use, this enzyme is useful for enzymatic synthesis of sialic acid.
Used in the Sialic Acid Quantification Kit, SIALIC-Q

Propriétés physiques

Isoelectric point: 4.6 ± 0.1
Michaelis constant: 2.5 x 10‾3M (N-Acetylneuraminic acid)
Structure: 3 subunits (approx. 35,000) per mol of enzyme
Inhibitors: p-Chloromercuribenzoate, sodium dodecyl sulfact, Hg++, Ag+
Optimum pH: 7.5– 8.0
Optimum temp: 70°C
pH Stability: pH 6.0–9.0 (10°C, 25hr)
Thermal stability: Below 65°C (pH 7.5, 30 min)

Définition de l'unité

One unit will release 1.0 μmole of pyruvate from NANA per min at pH 7.7 at 37 °C.

Forme physique

Lyophilized powder containing mannitol and EDTA

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Yinan Zhang et al.
Applied microbiology and biotechnology, 86(2), 481-489 (2009-11-06)
N-acetyl-D-neuraminic acid (Neu5Ac) is a precursor for producing many pharmaceutical drugs such as zanamivir which have been used in clinical trials to treat and prevent the infection with influenza virus, such as the avian influenza virus H5N1 and the current
Sean R A Devenish et al.
Biochemical and biophysical research communications, 388(1), 107-111 (2009-08-04)
As part of a general study into the impact of quaternary structure on enzyme function, a library of 31 point mutations were engineered at the dimer-dimer interface of the homotetrameric (beta/alpha)(8)-barrel protein, N-acetylneuraminate lyase (NAL, EC 4.1.3.3). Disruption of the
Jacqueline Vogel-Scheel et al.
Applied and environmental microbiology, 76(15), 5181-5187 (2010-06-22)
To study the adaptation of an intestinal bacterium to its natural environment, germfree mice were associated with commensal Escherichia coli MG1655. Two-dimensional gel electrophoresis was used to identify proteins differentially expressed in E. coli MG1655 collected from either cecal contents
Chung-Hsien Cheng et al.
Microbial cell factories, 9, 63-63 (2010-08-31)
Overexpression of recombinant proteins usually triggers the induction of heat shock proteins that regulate aggregation and solubility of the overexpressed protein. The two-dimensional gel electrophoresis (2-DE)-mass spectrometry approach was used to profile the proteome of Escherichia coli overexpressing N-acetyl-D-glucosamine 2-epimerase
Ivan Campeotto et al.
Journal of molecular biology, 404(1), 56-69 (2010-09-10)
The substrate specificity of Escherichia coli N-acetylneuraminic acid lyase was previously switched from the natural condensation of pyruvate with N-acetylmannosamine, yielding N-acetylneuraminic acid, to the aldol condensation generating N-alkylcarboxamide analogues of N-acetylneuraminic acid. This was achieved by a single mutation
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