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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

Synonyme(s) :

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

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About This Item

Numéro de classification (Commission des enzymes):
4.1.3.3 (BRENDA, IUBMB)
Numéro MDL:
MFCD00131656
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli BL21

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

≥3.0 units/mg protein

Poids mol.

33.4 kDa

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

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.

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.

Définition de l'unité

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.

Forme physique

Lyophilized powder containing Tris-HCl and NaCl

Remarque sur l'analyse

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.

Pictogrammes

Exclamation mark
GHS07

Mention d'avertissement

Warning

Mentions de danger

H315,H319,H335

Conseils de prudence

P261 - P305 + P351 + P338

Classification des risques

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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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