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Literature summary for 5.1.3.7 extracted from

  • Beerens, K.; Soetaert, W.; Desmet, T.
    Characterization and mutational analysis of the UDP-Glc(NAc) 4-epimerase from Marinithermus hydrothermalis (2013), Appl. Microbiol. Biotechnol., 97, 7733-7740.
    View publication on PubMed
Search for more literature for 5.1.3.7

Cloned(Commentary)

Cloned (Comment) Organism
gene galE, expression of N-termminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Marinithermus hydrothermalis

Protein Variants

Protein Variants Comment Organism
G118A/G119A site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates Marinithermus hydrothermalis
G188S/G119S site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates Marinithermus hydrothermalis
S116A site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates Marinithermus hydrothermalis
S279Y site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates Marinithermus hydrothermalis
T117S site-directed mutagenesis, the mutant shows highly reduced activity with UDP-N-acetylglucosamine and reduced activity with UDP-Gal, the mutant's substrate specificity is shifted toward non-acetylated substrates Marinithermus hydrothermalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.519
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, wild-type enzyme Marinithermus hydrothermalis
0.578
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant S116A Marinithermus hydrothermalis
0.887
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant T117S Marinithermus hydrothermalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-alpha-D-glucosamine Marinithermus hydrothermalis
-
 UDP-N-acetyl-alpha-D-galactosamine
-
 ?

Organism

Organism UniProt Comment Textmining
Marinithermus hydrothermalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-termminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Marinithermus hydrothermalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is active on both acetylated and non-acetylated UDP-hexoses, see for EC 5.1.3.2 Marinithermus hydrothermalis ?
-
 ?
UDP-N-acetyl-alpha-D-glucosamine
-
 Marinithermus hydrothermalis UDP-N-acetyl-alpha-D-galactosamine
-
 ?

Subunits

Subunits Comment Organism
More sequence comparisons and structure homology modeling, overview. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine Marinithermus hydrothermalis

Synonyms

Synonyms Comment Organism
GalE
-
 Marinithermus hydrothermalis
UDP-Glc(NAc) 4-epimerase
-
 Marinithermus hydrothermalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
-
 Marinithermus hydrothermalis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 half-life is 13.5 h Marinithermus hydrothermalis
60
-
 half-life is 23 min Marinithermus hydrothermalis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.58
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, wild-type enzyme Marinithermus hydrothermalis
0.83
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant T117S Marinithermus hydrothermalis
1
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant S116A Marinithermus hydrothermalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5
-
 Marinithermus hydrothermalis

pH Range

pH Minimum pH Maximum Comment Organism
6 9 over 50% of maximal activity at pH 6.0 and pH 9.0 Marinithermus hydrothermalis

General Information

General Information Comment Organism
evolution UDP-hexose 4-epimerases belong to the superfamily of short-chain dehydrogenase/reductase group 2, which typically show a two-domain structure Marinithermus hydrothermalis
additional information structure homology modeling, overview. The Marinithermus enzyme makes use of a TxnYx3K catalytic triad rather than the usual SxnYx3K triad. The enzyme's catalytic triad contains a threonine residue (Thr117) instead of the usual serine, the gatekeeper residue is responsible for the substrate specificity, the two consecutive glycine residues, Gly118 and Gly119, are a unique feature of GalE enzymes from Thermus species and important for activity as well as affinity Marinithermus hydrothermalis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.93
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant T117S Marinithermus hydrothermalis
1.11
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, wild-type enzyme Marinithermus hydrothermalis
1.73
-
 UDP-N-acetyl-alpha-D-glucosamine pH 7.5, 45°C, mutant S116A Marinithermus hydrothermalis