Native Microorganism N-Acetylneuraminic acid aldolase
| Cat# | DIA-182 |
| Source | Microorganism |
| Description | In enzymology, a N-acetylneuraminate lyase (EC 4.1.3.3) is an enzyme that catalyzes the chemical reaction: N-acetylneuraminate ↔ N-acetyl-D-mannosamine + pyruvate. Hence, this enzyme has one substrate, N-acetylneuraminate, and two products, N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. |
| Form | Freeze dried powder |
| Activity | Grade III 15U/mg-solid or more (30U/mg-protein or more), (containing approx. 30% of stabilizers) |
| CAS No. | 9027-60-5 |
| Isoelectric point | 4.6±0.1 |
| Synonyms | N-Acetylneuraminate Pyruvate Lyase; N-Acetylneuraminic Acid Lyase; NANA Aldolase; EC 4.1.3.3; N-acetylneuraminate pyruvate-lyase (N-acetyl-D-mannosamine-forming); N-acetylneuraminic acid aldolase; acetylneuraminate lyase; sialic aldolase; sialic acid aldolase; sialate lyase; N-acetylneuraminic aldolase; neuraminic aldolase; N-acetylneuraminate aldolase; neuraminic acid aldolase; N-acetylneuraminic acid aldolase; neuraminate aldolase; N-acetylneuraminic lyase; NPL; NALase; NANA lyase; acetylneuraminate pyruvate-lyase; N-acetylneuraminate pyruvate-lyase |
| Enzyme Commission Number | EC 4.1.3.3 |
| pH Stability | pH 6.0−9.0 (10°C, 25hr) |
| Michaelis Constant | 2.5×10⁻³M (N-Acetylneuraminic acid) |
| Optimum pH | 7.5-8.0 |
| Optimum temperature | 70°C |
| Thermal stability | below 65°C (pH 7.5, 30min) |
| Stability | Stable at-20°C for at least 6 months |
| Inhibitors | p-Chloromercuribenzoate, sodium dodecyl sulfate, Hg⁺⁺, Ag⁺ |
| Contaminants | Catalase < 1.0%, NADH oxidase < 1.0x10⁻³% |
| Abbr | NALase (Microorganism) |
| Alias | NPL; NALase; NANA lyase |
| Applications | 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. |
| Appearance | Yellowish amorphous powder, lyophilized |
| Structure | 3 subunits (approx. 35,000) per mol of enzyme |
| Molecular Weight | approx. 98 kDa |
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