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Literature summary for 5.1.3.3 extracted from

  • Beebe, J.A.; Frey, P.A.
    Galactose mutarotase: purification, characterization, and investigations of two important histidine residues (1998), Biochemistry, 37, 14989-14997.
    View publication on PubMed
Search for more literature for 5.1.3.3

Protein Variants

Protein Variants Comment Organism
H104Q about 600fold increase in Km-value Escherichia coli
H175N no enzymic activity detected Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diethyldicarbonate complete loss of activity, galactose partly saves Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
17
-
 alpha-D-glucose mutant H104Q, pH 7.5, 27°C Escherichia coli
29
-
 alpha-D-glucose wild-type, pH 7.5, 27°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no metal ion found Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucose = beta-D-glucose concerted general acid/general base mechanism Escherichia coli
a

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
27
-
 pH 6.0, full activity for at least 4.8 h Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3300
-
 alpha-D-glucose mutant H104Q, pH 7.5, 27°C Escherichia coli
22000
-
 alpha-D-glucose wild-type, pH 7.5, 27°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information no oxidoreduction cofactor Escherichia coli