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Literature summary for 4.1.3.3 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)

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

Protein Variants

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

KM Value [mM]

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

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
NAL
-
Escherichia coli

Temperature Stability [°C]

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

Turnover Number [1/s]

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

General Information

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