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Literature summary extracted from

  • Fukasawa, T.; Segawa, T.; Nogi, Y.
    Uridine diphosphate glucose-4-epimerase and galactose-1-phosphate uridylyltransferase from Saccharomyces cerevisiae (1982), Methods Enzymol., 89, 584-592.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.2 p-chloromercuribenzoate
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.12 0.2 0.26 UDP-glucose pH 8.7, 25°C Saccharomyces cerevisiae
5.1.3.2 0.22
-
 UDPgalactose
-
 Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.12 38000
-
 2 * 38000, SDS-PAGE Saccharomyces cerevisiae
2.7.7.12 86100
-
 sedimentation equilibrium centrifugation Saccharomyces cerevisiae
5.1.3.2 78000
-
 2 * 78000, SDS-PAGE Saccharomyces cerevisiae
5.1.3.2 183000 187000 sucrose density gradient centrifugation, gel filtration Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.12 Saccharomyces cerevisiae
-
-
-
2.7.7.12 Saccharomyces cerevisiae 106-3D
-
-
-
5.1.3.2 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.12
-
 Saccharomyces cerevisiae
5.1.3.2
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.12 54.1
-
 purified enzyme Saccharomyces cerevisiae
5.1.3.2 31.8
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.12 UDP-glucose + alpha-D-galactose 1-phosphate
-
 Saccharomyces cerevisiae alpha-D-glucose 1-phosphate + UDP-galactose
-
 r
2.7.7.12 UDP-glucose + alpha-D-galactose 1-phosphate
-
 Saccharomyces cerevisiae 106-3D alpha-D-glucose 1-phosphate + UDP-galactose
-
 r
5.1.3.2 UDP-galactose
-
 Saccharomyces cerevisiae UDP-glucose
-
 ?
5.1.3.2 UDP-galactose
-
 Saccharomyces cerevisiae 106-3D UDP-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.12 dimer 2 * 38000, SDS-PAGE Saccharomyces cerevisiae
5.1.3.2 dimer 2 * 78000, SDS-PAGE Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.12 27
-
 assay at Saccharomyces cerevisiae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.7.12 additional information
-
 activation energy, temperature profile Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.3.2 30
-
 53% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM Saccharomyces cerevisiae
5.1.3.2 37
-
 85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.12 987
-
 alpha-D-galactose 1-phosphate pH 8.7, 25°C Saccharomyces cerevisiae
5.1.3.2 64.8
-
 UDPgalactose
-
 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.12 8.4 8.8
-
 Saccharomyces cerevisiae
5.1.3.2 7.3
-
-
 Saccharomyces cerevisiae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.12 7.1 9.4 56% of maximal activity at pH 7.1 and 83% of maximal activity at pH 9.4 Saccharomyces cerevisiae
5.1.3.2 6.7 8.1 6.7: 91% of maximal activity, 8.1: 88% of maximal activity Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
5.1.3.2 NAD+ each dimer contains one molecule of NAD+ tightly bound Saccharomyces cerevisiae