ec 4.1.3.3 structure
|
Common Name | ec 4.1.3.3 | ||
---|---|---|---|---|
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 |
---|---|
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]. |
---|---|
Related Catalog | |
References |
Density | 1.000 g/cm3 |
---|---|
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) |
---|---|
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 |
Chemistry, metabolism, and biological functions of sialic acids.
Adv. Carbohydr. Chem. Biochem. 40 , 131, (1982)
|
|
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... |
|
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 |