ec 4.1.3.3
ec 4.1.3.3 structure
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Common Name | ec 4.1.3.3 | ||
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| CAS Number | 9027-60-5 | Molecular Weight | 398.583 | |
| Density | 1.000 g/cm3 | Boiling Point | N/A | |
| Molecular Formula | C23H42O5 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
Use of ec 4.1.3.3N-Acetylneuraminic acid lyase (NAL) is a class I aldolase, is often used in biochemical studies. N-Acetylneuraminic acid lyase catalyzes the reversible condensation of pyruvate with N-acetyl-d-mannosamine (ManNAc) to yield the sialic acid N-acetylneuraminic acid (Neu5Ac)[1]. |
| Name | N-Acetylneuraminic Acid Aldolase,from Microorganism |
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| Synonym | More Synonyms |
| Description | N-Acetylneuraminic acid lyase (NAL) is a class I aldolase, is often used in biochemical studies. N-Acetylneuraminic acid lyase catalyzes the reversible condensation of pyruvate with N-acetyl-d-mannosamine (ManNAc) to yield the sialic acid N-acetylneuraminic acid (Neu5Ac)[1]. |
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| Related Catalog | |
| References |
| Density | 1.000 g/cm3 |
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| Molecular Formula | C23H42O5 |
| Molecular Weight | 398.583 |
| Appearance of Characters | powder | slightly yellow |
| Storage condition | −20°C |
| Personal Protective Equipment | Eyeshields;Gloves;half-mask respirator (US);multi-purpose combination respirator cartridge (US) |
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| Hazard Codes | Xi |
| Risk Phrases | 36/37/38 |
| Safety Phrases | 23-24/25-60-37-26-22 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | 3 |
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Chemistry, metabolism, and biological functions of sialic acids.
Adv. Carbohydr. Chem. Biochem. 40 , 131, (1982)
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Structural basis for substrate specificity and mechanism of N-acetyl-D-neuraminic acid lyase from Pasteurella multocida.
Biochemistry 52(47) , 8570-9, (2013) N-Acetylneuraminate lyases (NALs) or sialic acid aldolases catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac, the most common form of sialic acid) to form pyruvate and N-acetyl... |
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Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with γ-thialysine by using a chemical mutagenesis strategy.
ChemBioChem. 14(4) , 474-81, (2013) Chemical modification has been used to introduce the unnatural amino acid γ-thialysine in place of the catalytically important Lys165 in the enzyme N-acetylneuraminic acid lyase (NAL). The Staphylococ... |
| MFCD00131656 |