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Literature summary extracted from

  • Agarwal, S.; Mishra, N.; Agarwal, S.; Dixit, A.
    Characterization of the active site and coenzyme binding pocket of the monomeric UDP-galactose 4'-epimerase of Aeromonas hydrophila (2010), BMB Rep., 43, 419-426.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.1.3.2 K153N the mutation affects the catalytic activity only slightly, however, the NAD+ binding potential is reduced dramatically Aeromonas hydrophila
5.1.3.2 Y149G the mutant is completely inactive Aeromonas hydrophila
5.1.3.2 Y149G/K153N the mutant is completely inactive Aeromonas hydrophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.2 diethyldicarbonate almost complete inhibition at 5 mM after 30 min incubation Aeromonas hydrophila

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.2 0.5
-
 UDP-galactose wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 0.8
-
 UDP-galactose mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 1
-
 UDP-galactose mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
5.1.3.2 diethyldicarbonate incubation of the recombinant His6-tagged protein with increasing concentrations of diethyldicarbonate (1.0-5.0 mM) results in a time-dependent loss of activity Aeromonas hydrophila
5.1.3.2 Glycerol the use of glycerol as a cosolvent enhances the GalE thermostability significantly. The enzyme in 50% glycerol can retain 90% of its activity, whereas only 20% activity is observed for the identically treated control enzyme Aeromonas hydrophila

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.2 Aeromonas hydrophila
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.2 UDP-alpha-D-glucose
-
 Aeromonas hydrophila UDP-alpha-D-galactose
-
 ?
5.1.3.2 UDP-galactose
-
 Aeromonas hydrophila UDP-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.3.2 monomer
-
 Aeromonas hydrophila

Synonyms

EC Number Synonyms Comment Organism
5.1.3.2 GalE
-
 Aeromonas hydrophila
5.1.3.2 UDP-galactose 4'-epimerase
-
 Aeromonas hydrophila

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.2 47
-
 the melting temperature of the recombinant enzyme is at 47°C Aeromonas hydrophila

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.2 0.633
-
 UDP-galactose mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 46
-
 UDP-galactose mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 116
-
 UDP-galactose wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.3.2 NAD+
-
 Aeromonas hydrophila

General Information

EC Number General Information Comment Organism
5.1.3.2 physiological function GalE plays a key role in lipopolysaccharide biosynthesis Aeromonas hydrophila

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.1.3.2 0.79
-
 UDP-galactose mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 46
-
 UDP-galactose mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila
5.1.3.2 232
-
 UDP-galactose wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C Aeromonas hydrophila