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Literature summary extracted from

  • Beebe, J.A.; Arabshahi, A.; Clifton, J.G.; Ringe, D.; Petsko, G.A.; Frey, P.A.
    Galactose mutarotase: pH dependence of enzymatic mutarotation (2003), Biochemistry, 42, 4414-4420.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.3.3 4
-
 alpha-D-galactose pH 7.0, 25°C Escherichia coli
5.1.3.3 38
-
 alpha-D-glucose pH 7.0, 25°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.3 Escherichia coli P0A9C3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.3.3 alpha-D-glucose = beta-D-glucose mechanism, one of the catalytic groups H104, H175, or E309, shuttles a proton to and from the endocyclic oxygen and the other two shuttle protons to the anomeric oxygen atoms. Ring opening of alpha-D-glucose limits the rate at low pH, but ring closure does not become rate limiting at pH up to 8.5 Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.3 alpha-D-galactose
-
 Escherichia coli beta-D-galactose
-
 ?
5.1.3.3 alpha-D-glucose
-
 Escherichia coli beta-D-glucose
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.3.3 additional information
-
 additional information turnover number is not dependent on pH-value Escherichia coli
5.1.3.3 18400
-
 alpha-D-galactose pH 7.0, 25°C Escherichia coli
5.1.3.3 19000
-
 alpha-D-glucose pH 7.0, 25°C Escherichia coli