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Literature summary extracted from

  • Lee, Y.C.; Chien, H.C.; Hsu, W.H.
    Production of N-acetyl-D-neuraminic acid by recombinant whole cells expressing Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase and Escherichia coli N-acetyl-D-neuraminic acid lyase (2007), J. Biotechnol., 129, 453-460.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.1.3.8 ADP 20 fold increase in activity Anabaena sp. CH1
5.1.3.8 AMPPNP 20 fold increase in activity Anabaena sp. CH1
5.1.3.8 ATP 0.180 mM for maximal activity Sus scrofa
5.1.3.8 ATP 20 fold increase in activity, 0.020 mM for maximal activity Anabaena sp. CH1
5.1.3.8 dATP 20 fold increase in activity Anabaena sp. CH1

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.3 expressed in Escherichia coli BL21 (DE3) cells Escherichia coli
5.1.3.8 expression in Escherichia coli Anabaena sp. CH1

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.8 pyruvate 50% reduced activity at 0.2 M pyruvate Anabaena sp. CH1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.8 25.4
-
N-acetyl-D-mannosamine
-
Anabaena sp. CH1

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.8 Mg2+
-
Sus scrofa
5.1.3.8 Mg2+ no effect Anabaena sp. CH1

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.3.3 33000
-
SDS-PAGE Escherichia coli
5.1.3.8 42000
-
calculated, SDS-PAGE Anabaena sp. CH1

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.3 Escherichia coli
-
-
-
5.1.3.8 Anabaena sp. CH1 A4UA16
-
-
5.1.3.8 Sus scrofa P17560
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.3 Ni-NTA column chromatography Escherichia coli
5.1.3.8 of the recombinant protein by immobilized nickel-ion chromatography Anabaena sp. CH1

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.1.3.8 kidney
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.3.8 32
-
in the presence of 1 mM ATP Sus scrofa
5.1.3.8 124
-
in the presence of 1 mM ATP Anabaena sp. CH1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.3 N-acetyl-neuraminic acid
-
Escherichia coli N-acetyl-D-mannosamine + pyruvate
-
r
5.1.3.8 N-acetyl-D-glucosamine
-
Sus scrofa N-acetyl-D-mannosamine
-
r
5.1.3.8 N-acetyl-D-glucosamine
-
Anabaena sp. CH1 N-acetyl-D-mannosamine
-
r

Synonyms

EC Number Synonyms Comment Organism
4.1.3.3 N-acetyl-D-neuraminic acid lyase
-
Escherichia coli
4.1.3.3 NeuAc lyase
-
Escherichia coli
5.1.3.8 AGE
-
Sus scrofa
5.1.3.8 AGE
-
Anabaena sp. CH1
5.1.3.8 bGlcNAc 2-epimerase recombinant protein Sus scrofa
5.1.3.8 bGlcNAc 2-epimerase recombinant protein Anabaena sp. CH1
5.1.3.8 GlcNAc 2-epimerase
-
Sus scrofa
5.1.3.8 GlcNAc 2-epimerase
-
Anabaena sp. CH1
5.1.3.8 N-acyl-D-glucosamine 2-epimerase
-
Sus scrofa
5.1.3.8 N-acyl-D-glucosamine 2-epimerase
-
Anabaena sp. CH1
5.1.3.8 N-acylglucosamine 2-epimerase
-
Sus scrofa
5.1.3.8 N-acylglucosamine 2-epimerase
-
Anabaena sp. CH1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.3.8 50
-
-
Anabaena sp. CH1

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.3.8 35 55 more than 90% of maximal activity Anabaena sp. CH1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.8 7
-
-
Anabaena sp. CH1

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.3.8 7 9.5 more than 90% of maximal activity Anabaena sp. CH1