A6680
N-Acetylneuraminic Acid Aldolase from microorganisms
lyophilized powder, ≥20 units/mg protein (biuret)
Synonym(s):
N-Acetylneuraminate Pyruvate Lyase, N-Acetylneuraminic Acid Lyase, NANA Aldolase, Sialic Aldolase
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All Photos(5)
About This Item
CAS Number:
Beilstein:
2697172
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32
Recommended Products
form
lyophilized powder
specific activity
≥20 units/mg protein (biuret)
mol wt
~98 kDa
storage temp.
−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.
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
Physical properties
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)
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)
Unit Definition
One unit will release 1.0 μmole of pyruvate from NANA per min at pH 7.7 at 37 °C.
Physical form
Lyophilized powder containing mannitol and EDTA
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Vera Zimmermann et al.
Applied microbiology and biotechnology, 76(3), 597-605 (2007-07-03)
In this work, a model describing the complete enzyme catalysed synthesis of N-acetylneuraminic acid (Neu5Ac) from N-acetyl-D-glucosamine (GlcNAc) is presented. It includes the combined reaction steps of epimerisation from GlcNAc to N-acetyl-D-mannosamine (ManNAc) and the aldol condensation of ManNAc with
Varun Bhaskar et al.
Proteins, 79(4), 1132-1142 (2011-02-05)
YagE is a 33 kDa prophage protein encoded by CP4-6 prophage element in Escherichia coli K12 genome. Here, we report the structures of YagE complexes with pyruvate (PDB Id 3N2X) and KDGal (2-keto-3-deoxy galactonate) (PDB Id 3NEV) at 2.2A resolution.
Shiyuan Hu et al.
Applied microbiology and biotechnology, 85(5), 1383-1391 (2009-08-27)
N-Acetyl-D: -neuraminic acid (Neu5Ac) can be produced from N-acetyl-D: -glucosamine (GlcNAc) and pyruvate by a chemoenzymatic process in which an alkaline-catalyzed epimerization transforms GlcNAc to N-acetyl-D: -manosamine (ManNAc). ManNAc is then condensed biocatalytically with pyruvate in the presence of N-acetyl-D:
Xiaoman Xu et al.
Applied and environmental microbiology, 77(10), 3197-3201 (2011-03-29)
Production of N-acetyl-D-neuraminic acid (Neu5Ac) via biocatalysis is traditionally conducted using isolated enzymes or whole cells. The use of isolated enzymes is restricted by the time-consuming purification process, whereas the application of whole cells is limited by the permeability barrier
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
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