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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(e):

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

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About This Item

EC-Nummer:
4.1.3.3 (BRENDA, IUBMB)
MDL-Nummer:
MFCD00131656
UNSPSC-Code:
12352204
NACRES:
NA.54

Rekombinant

expressed in E. coli BL21

Qualitätsniveau

200

Form

lyophilized powder

Spezifische Aktivität

≥3.0 units/mg protein

Mol-Gew.

33.4 kDa

Versandbedingung

dry ice

Lagertemp.

−20°C

Allgemeine Beschreibung

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.

Anwendung

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.

Einheitendefinition

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.

Physikalische Form

Lyophilized powder containing Tris-HCl and NaCl

Hinweis zur 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.

Piktogramme

Exclamation mark
GHS07

Signalwort

Warning

Gefahreneinstufungen

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

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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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
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
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

Artikel

Sialic Acid

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