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Literature summary extracted from

  • Devenish, S.R.; Gerrard, J.A.
    The quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression (2009), Biochem. Biophys. Res. Commun., 388, 107-111.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.3 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.3 I229D the mutant shows decreased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 I229N the mutant shows increased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 I229R the mutant shows increased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L171D the mutant is insoluble Escherichia coli
4.1.3.3 L171D/L199D/I229D the mutant is insoluble Escherichia coli
4.1.3.3 L171D/L199N/I229D the mutant is insoluble Escherichia coli
4.1.3.3 L171N the mutant is insoluble Escherichia coli
4.1.3.3 L171N/I229N the mutant shows decreased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L171R the mutant shows decreased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L171R/L199N/I229R the mutant is insoluble Escherichia coli
4.1.3.3 L171R/L199R/I229R the mutant is insoluble Escherichia coli
4.1.3.3 L199D the mutant is insoluble Escherichia coli
4.1.3.3 L199N the mutant shows increased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L199N/I229D the mutant shows decreased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L199N/I229N the mutant shows decreased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L199N/I229R the mutant shows increased kcat compared to the wild type enzyme Escherichia coli
4.1.3.3 L199R the mutant is insoluble Escherichia coli
4.1.3.3 L199R/I229N the mutant shows increased kcat compared to the wild type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.3.3 2.51
-
 N-acetylneuraminate mutant enzyme L171N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 3.2
-
 N-acetylneuraminate mutant enzyme L199N/I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 3.4
-
 N-acetylneuraminate mutant enzyme I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 3.42
-
 N-acetylneuraminate mutant enzyme L171R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 3.93
-
 N-acetylneuraminate mutant enzyme I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 4
-
 N-acetylneuraminate mutant enzyme L199N/I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 4.1
-
 N-acetylneuraminate wild type enzyme, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 4.3
-
 N-acetylneuraminate mutant enzyme L199N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 4.7
-
 N-acetylneuraminate mutant enzyme L199N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 5
-
 N-acetylneuraminate mutant enzyme I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 6.1
-
 N-acetylneuraminate mutant enzyme L199R/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.3.3 35000
-
 4 * 35000, His-tagged enzyme, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.3 Escherichia coli P0A6L4
-
-
4.1.3.3 Escherichia coli W3110 / ATCC 27325 P0A6L4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.3 HisTrap column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.3 N-acetylneuraminate
-
 Escherichia coli N-acetyl-D-mannosamine + pyruvate
-
 r
4.1.3.3 N-acetylneuraminate
-
 Escherichia coli W3110 / ATCC 27325 N-acetyl-D-mannosamine + pyruvate
-
 r

Subunits

EC Number Subunits Comment Organism
4.1.3.3 homotetramer 4 * 35000, His-tagged enzyme, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.1.3.3 NAL
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.3.3 84
-
 the melting temperature of the wild type enzyme is at 84°C Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.3.3 0.29
-
 N-acetylneuraminate mutant enzyme L199N/I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 0.664
-
 N-acetylneuraminate mutant enzyme L199N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 3.15
-
 N-acetylneuraminate mutant enzyme L171N/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 4.69
-
 N-acetylneuraminate mutant enzyme I229D, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 5.49
-
 N-acetylneuraminate mutant enzyme L171R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 6.75
-
 N-acetylneuraminate wild type enzyme, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 7.4
-
 N-acetylneuraminate mutant enzyme I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 7.72
-
 N-acetylneuraminate mutant enzyme I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 7.94
-
 N-acetylneuraminate mutant enzyme L199N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 8.9
-
 N-acetylneuraminate mutant enzyme L199N/I229R, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli
4.1.3.3 11.87
-
 N-acetylneuraminate mutant enzyme L199R/I229N, in sodium phosphate buffer (100 mM, pH 7.6), at 30°C Escherichia coli

General Information

EC Number General Information Comment Organism
4.1.3.3 physiological function the quaternary structure of Escherichia coli N-acetylneuraminate lyase is essential for functional expression Escherichia coli