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A6680

Sigma-Aldrich

N-Acetylneuraminic Acid Aldolase from microorganisms

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

Synonyma:

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

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
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About This Item

Číslo CAS:
9027-60-5
Číslo enzymu podle klasifikace EK:
4.1.3.3 (BRENDA, IUBMB)
Beilstein/REAXYS Number:
2697172
MDL number:
MFCD00131656
UNSPSC Code:
12352204
NACRES:
NA.32

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.
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)

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

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Sigma-Aldrich

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Sigma-Aldrich

N8129

β-Nicotinamide adenine dinucleotide, reduced disodium salt hydrate

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.
Yanhong Li et al.
Applied microbiology and biotechnology, 79(6), 963-970 (2008-06-04)
Sialic acid aldolases or N-acetylneuraminate lyases (NanAs) catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-D: -mannosamine (ManNAc). A capillary electrophoresis assay was developed to directly characterize the activities of NanAs in both Neu5Ac cleavage
Hee Gon Jeong et al.
Infection and immunity, 77(8), 3209-3217 (2009-06-03)
N-acetylneuraminic acid (Neu5Ac, sialic acid) could provide a good substrate for enteropathogenic bacteria in the intestine, when the bacteria invade and colonize in human gut. In order to analyze the role of Neu5Ac catabolism in Vibrio vulnificus pathogenesis, a mutant
Wen-liu Yang et al.
Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences, 39(1), 57-63 (2010-02-23)
To obtain the Escherichia coli strains expressing N-Acetyl-D-neuraminic acid aldolase (Neu5Ac aldolase). The gene (nanA) coding Neu5Ac aldolase was cloned from Escherichia coli C600, and the recombinant plasmid was sequenced and expressed in Escherichia coli. Sequencing data revealed that the
Jozef Nahálka et al.
Journal of biotechnology, 134(1-2), 146-153 (2008-03-04)
The propensity of a recombinant protein produced in bacteria to aggregate has been assumed to be unpredictable, and inclusion bodies have been thought of as wasted cell material. However, a target protein can be purposely driven to inclusion bodies, which
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