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4.1.3.3: N-acetylneuraminate lyase

This is an abbreviated version!
For detailed information about N-acetylneuraminate lyase, go to the full flat file.

Word Map on EC 4.1.3.3

Reaction

aceneuramate
=
N-acetyl-D-mannosamine
+
pyruvate

Synonyms

Acetylneuraminate pyruvate-lyase, class I NAL, EcNanA, Lyase, acetylneuraminate, N-acetyl-d-neuraminic acid aldolase, N-acetyl-D-neuraminic acid lyase, N-Acetylneuraminate aldolase, N-Acetylneuraminate lyase, N-acetylneuraminate pyruvate lyase, N-Acetylneuraminate pyruvate-lyase, N-Acetylneuraminic acid aldolase, N-Acetylneuraminic acid lyase, N-Acetylneuraminic aldolase, N-Acetylneuraminic lyase, NAL, NALase, NanA, NANA lyase, Neu5Ac aldolase, Neu5Ac lyase, NeuAc aldolase, NeuAc lyase, Neuraminate aldolase, Neuraminic acid aldolase, Neuraminic aldolase, NPL, PmNanA, sialate aldolase, Sialate lyase, sialate-pyruvate lyase, Sialic acid aldolase, Sialic aldolase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.3 N-acetylneuraminate lyase

Crystallization

Crystallization on EC 4.1.3.3 - N-acetylneuraminate lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
L142R mutant, complexed with beta-hydroxypyruvate, hanging drop vapor diffusion method
mutant enzyme E192N, in complex with pyruvate, sitting drop vapor diffusion method, using 100 mM Tris-HCl pH 8.2, 200 mM ammonium acetate, 18% PEG 3350
sitting drop diffusion method, PEG 3350
-
complexed with sialic acid alditol, 4-deoxy-sialic acid or 4-oxo-sialic acid, microbatch crystallization, hanging drop vapor diffusion method
-
recombinant enzyme in complex with N-acetylneuraminate and acetyl-D-mannosamine/pyruvate, soaking in the mother liquor containing 15% w/v PEG400, then 20% w/v PEG400, and subsequently for 5 min in 25% w/v PEG400 containing 75 mM Neu5Ac, X-ray diffraction structure determination and analysis
-
purified recombinant His-tagged wild-type enzyme, wild-type enzyme with Schiff base and in complex with pyruvate, mutant K164A enzyme, and mutant K164A in complex with N-acetylneuraminic acid and N-glycolylneuraminic acid, hanging drop vapour diffusion method, crystals of wild-type PmNAL from 21% PEG 1000, 150 mM NaCl, and 100 mM Na2HPO4/KH2PO4, pH 6.2. PmNAL K164A mutant in ligand-free from from 30% PEG 200, 100 mM NaCl, and acetate, pH 4.5. Crystals of the PmNAL K164A mutant bound to ligands are grown in 38% PEG 300, 0.01 M CaCl2, and 0.1 M sodium cacodylate, pH 6.5. The sialic acid concentration was 5 mM, X-ray diffraction structure determination and analysis at 1.75-2.10 A resolution, molecular replacement modeling
ligand-free and (2R)-sialic acid alditol-bound enzyme, hanging drop vapor diffusion method, using
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002-0.0025 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, is mixed with 0.0017-0.0022 ml of reservoir solution containing 25% w/v PEG 3350, 200 mM ammonium sulfate, 100 mM Bis-Tris pH 5.5, equilibration against 1 ml of reservoir solution, 8-20°C, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement
purified recombinant wild-type enzyme and mutants K165C variant and K165-gamma-thialysine, alone or in complex with pyruvate, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution containing 8 mg/ml protein in 50 mM, pH 7.4, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.0-8.5, 200 mM NaCl, and 18-28% w/v PEG 3350, pyruvate complexes of the wild-type and K165-gamma-thialysine mutant enzymes crystals are soaked in the mother liquor containing 100 mM sodium pyruvate and 15% v/v PEG 400 for 1 min before being sequentially transferred to mother liquor with 5% increments in PEG 400 concentration. The final soak contains the mother liquor containing 100 mM sodium pyruvate and 25% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at about 2.0 A resolution, molecular replacement