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S1826

Sigma-Aldrich

Sialic Acid Aldolase from Escherichia coli K12

recombinant, expressed in E. coli BL21, ≥3.0 units/mg protein

Synonym(s):

N-Acetylneuraminate lyase, N-Acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming)

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10 UNITS
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10 UNITS
$353.70

About This Item

Enzyme Commission number:
4.1.3.3 (BRENDA, IUBMB)
MDL number:
MFCD00131656
UNSPSC Code:
12352204
NACRES:
NA.54

$353.70

List Price$393.00Save 10%
Web-Only Promotion
Check Cart for Availability

recombinant

expressed in E. coli BL21

Quality Level

200

form

lyophilized powder

specific activity

≥3.0 units/mg protein

mol wt

33.4 kDa

shipped in

dry ice

storage temp.

−20°C

General description

Sialic acid aldolases, or N-acetylneuraminate lyases, catalyze the reversible aldol cleavage of N-acetylneuraminic acid to form pyruvate and N-acetyl-D-mannosamine. In nature, N-acetylneuraminate lyase mainly occurs in pathogens. [1]

Application

Sialic acid aldolase can be used to synthesize unnatural sugars of C(6) to C(10) for the design of antagonists and inhibitors of glycoenzymes. [2]

Unit Definition

One unit will catalyze the formation of 1.0 μmol Neu-5-Ac from Man-N-Ac and pyruvate per minute at 37°C at pH 8.0.

Physical form

Lyophilized powder containing Tris-HCl and NaCl

Analysis Note

Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 7.5) containing Neu-5-Ac (10 mM) at 37 °C for 15 min and analyzed using capillary electrophoresis with UV detection at 200 nm.

pictograms

Exclamation mark
GHS07

signalword

Warning

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000435713
0000435713
0000371704
0000371704
0000300733

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Chien-Yu Chou et al.
The Journal of biological chemistry, 286(16), 14057-14064 (2011-01-29)
In a recent directed-evolution study, Escherichia coli D-sialic acid aldolase was converted by introducing eight point mutations into a new enzyme with relaxed specificity, denoted RS-aldolase (also known formerly as L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase), which showed a preferred selectivity toward
Guiomar Sánchez-Carrón et al.
Applied and environmental microbiology, 77(7), 2471-2478 (2011-02-15)
N-Acetylneuraminate lyases (NALs) or sialic acid aldolases catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-d-mannosamine (ManNAc). In nature, N-acetylneuraminate lyase occurs mainly in pathogens. However, this paper describes how an N-acetylneuraminate lyase was cloned
Jozef Nahálka et al.
Organic & biomolecular chemistry, 7(9), 1778-1780 (2009-07-11)
Active inclusion bodies of polyphosphate kinase 3 and cytidine 5'-monophosphate kinase were combined with whole cells that co-express sialic acid aldolase and CMP-sialic acid synthetase. The biocatalytic mixture was used for the synthesis of CMP-sialic acid, which was then converted

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