ec 4.1.3.3
ec 4.1.3.3 structure
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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 | |
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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-d-mannosamine. Although equilibrium favors sialic acid cle... |
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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 Staphylococcus aureus nanA gene, encoding NAL, was cloned and expresse... |
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Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69(Pt 3) , 306-12, (2013) The enzyme N-acetylneuraminate lyase (EC 4.1.3.3) is involved in the metabolism of sialic acids. Specifically, the enzyme catalyzes the retro-aldol cleavage of N-acetylneuraminic acid to form N-acetyl-D-mannosamine and pyruvate. Sialic acids comprise a large ... |
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Production of N-acetyl-D-neuraminic acid using two sequential enzymes overexpressed as double-tagged fusion proteins.
BMC Biotechnol. 9 , 63, (2009) Two sequential enzymes in the production of sialic acids, N-acetyl-D-glucosamine 2-epimerase (GlcNAc 2-epimerase) and N-acetyl-D-neuraminic acid aldolase (Neu5Ac aldolase), were overexpressed as double-tagged gene fusions. Both were tagged with glutathione S-... |
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X-ray-excited optical luminescence of protein crystals: a new tool for studying radiation damage during diffraction data collection.
Acta Crystallogr. D Biol. Crystallogr. 68(Pt 5) , 505-10, (2012) During X-ray irradiation protein crystals radiate energy in the form of small amounts of visible light. This is known as X-ray-excited optical luminescence (XEOL). The XEOL of several proteins and their constituent amino acids has been characterized using the... |
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Blood-based biomarkers can differentiate ulcerative colitis from Crohn's disease and noninflammatory diarrhea.
Inflamm. Bowel Dis. 17(8) , 1719-25, (2011) Blood gene expression profiling has been used in several studies to identify patients with a number of conditions and diseases. A blood test with the ability to differentiate Crohn's disease (CD) from ulcerative colitis (UC) and noninflammatory diarrhea would... |
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The sialic acids. I. The structure and enzymatic synthesis of N-acetylneuraminic acid.
J. Biol. Chem. 235 , 2529-37, (1960)
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Asymmetric transformations involving 1,2-dicarbonyl compounds as pronucleophiles.
Chem. Commun. (Camb.) 48(54) , 6763-75, (2012) This article concentrates on the versatile nucleophilic reactivity of 1,2-dicarbonyl compounds in various asymmetric transformations. Although underexploited in comparison to their 1,3-dicarbonyl homologues, the presence of adjacent multiple reactive centres ... |
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Coupled bioconversion for preparation of N-acetyl-D: -neuraminic acid using immobilized N-acetyl-D: -glucosamine-2-epimerase and N-acetyl-D: -neuraminic acid lyase.
Appl. Microbiol. Biotechnol. 85(5) , 1383-91, (2010) N-Acetyl-D: -neuraminic acid (Neu5Ac) can be produced from N-acetyl-D: -glucosamine (GlcNAc) and pyruvate by a chemoenzymatic process in which an alkaline-catalyzed epimerization transforms GlcNAc to N-acetyl-D: -manosamine (ManNAc). ManNAc is then condensed ... |