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Literature summary for 5.1.3.2 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
Search for more literature for 5.1.3.2

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Organic Solvent Stability

Organic Solvent Comment Organism
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
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

Organism UniProt Comment Textmining
Aeromonas hydrophila
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
monomer
-
 Aeromonas hydrophila

Synonyms

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Aeromonas hydrophila

General Information

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

kcat/KM [mM/s]

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